{"title":"StressMarq Biosciences","description":"Products supplied by StressMarq Biosciences Inc.","products":[{"product_id":"hsp90-alpha-protein-bhp11900001","title":"HSP90 alpha Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP90 alpha\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSP90 alpha (source species: Human; native localization: Cytoplasm | Melanosome).\u003c\/p\u003e\u003cp\u003eHuman Recombinant HSP90 alpha Protein\u003c\/p\u003e\u003cp\u003eHSP90 alpha is a highly conserved molecular chaperone that plays a central role in maintaining protein homeostasis under both normal and stress conditions. In the context of neuroscience, HSP90 alpha is increasingly recognized for its involvement in the folding, stabilization, and functional regulation of key neuronal proteins, including kinases, transcription factors, and hormone receptors.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eMechanistically, \u003cstrong\u003eHSP90 alpha\u003c\/strong\u003e functions within the cellular proteostasis network, helping client proteins reach and maintain functional conformations under basal and stress conditions. Many clients are signaling proteins (e.g., kinases) whose stability and activity are sensitive to folding state and chaperone availability. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Melanosome\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~90 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 50mM Tris\/HCl pH7.5, 5mM Bme, 0.3M NaCl, 10% glycerol\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required. For molecular chaperones, nucleotide-binding state and co-chaperone interactions often shape functional readouts.\u003c\/p\u003e\u003ch2\u003eStructural and biochemical features\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eStructural\/biochemical context:\u003c\/strong\u003e Many chaperones cycle through nucleotide-bound conformations that regulate client binding and release. Co-chaperones can tune this cycle and change apparent interaction profiles in reconstituted assays.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Changes in chaperone abundance or activity can reflect altered proteostasis demand (e.g., heat shock, oxidative stress, proteotoxic challenge) and may shift the stability landscape of client proteins. Interpreting effects often benefits from pairing chaperone measurements with client-protein stability, stress-response transcriptional markers, and aggregation\/solubility readouts.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287347053,"sku":"SPR-101A","price":141.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287379821,"sku":"SPR-101B","price":235.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-101_HSP90-Alpha-Protein-SDS-Page-2.png?v=1770640174"},{"product_id":"hsp90-beta-protein-bhp11900004","title":"HSP90 beta Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP90 beta\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSP90 beta (source species: Human; native localization: Cytoplasm | Melanosome).\u003c\/p\u003e\u003cp\u003eHuman Recombinant HSP90 beta Full Length Protein\u003c\/p\u003e\u003cp\u003eHSP90 beta is the constitutively expressed isoform of the HSP90 family and is essential for the maintenance of cellular protein networks. In the nervous system, HSP90 beta supports the folding and maturation of proteins involved in synaptic transmission, cytoskeletal dynamics, and neuronal survival.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eMechanistically, \u003cstrong\u003eHSP90 beta\u003c\/strong\u003e functions within the cellular proteostasis network, helping client proteins reach and maintain functional conformations under basal and stress conditions. Many clients are signaling proteins (e.g., kinases) whose stability and activity are sensitive to folding state and chaperone availability. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Melanosome\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~90 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;85%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Baculovirus\/Sf9\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified | Low Endotoxin\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 20mM Tris, pH7.5, 175 mM NaCl, 0.1 mM EDTA, 10% glycerol, 1 mM DTT\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Insect-cell expression supports eukaryotic folding and some PTMs, which can be beneficial for structurally complex proteins. Glycan patterns may differ from mammalian cells and can influence certain binding-dependent assays. For molecular chaperones, nucleotide-binding state and co-chaperone interactions often shape functional readouts.\u003c\/p\u003e\u003ch2\u003eStructural and biochemical features\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eStructural\/biochemical context:\u003c\/strong\u003e Many chaperones cycle through nucleotide-bound conformations that regulate client binding and release. Co-chaperones can tune this cycle and change apparent interaction profiles in reconstituted assays.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Baculovirus\/Sf9. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified | Low Endotoxin. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Changes in chaperone abundance or activity can reflect altered proteostasis demand (e.g., heat shock, oxidative stress, proteotoxic challenge) and may shift the stability landscape of client proteins. Interpreting effects often benefits from pairing chaperone measurements with client-protein stability, stress-response transcriptional markers, and aggregation\/solubility readouts.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287412589,"sku":"SPR-102A","price":170.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287445357,"sku":"SPR-102B","price":289.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-102_HSP90-Beta-Protein-SDS-Page-2.png?v=1770640174"},{"product_id":"hsp70-protein-bhp11900007","title":"HSP70 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP70\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSP70 (source species: Human; native localization: Cytoplasm).\u003c\/p\u003e\u003cp\u003eHuman Recombinant HSP70 Protein\u003c\/p\u003e\u003cp\u003eHSP70 is a highly inducible molecular chaperone that plays a pivotal role in protein quality control across all major cellular compartments. In the brain, HSP70 is essential for preventing the aggregation of misfolded proteins, a key pathological feature of neurodegenerative diseases.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eMechanistically, \u003cstrong\u003eHSP70\u003c\/strong\u003e functions within the cellular proteostasis network, helping client proteins reach and maintain functional conformations under basal and stress conditions. Many clients are signaling proteins (e.g., kinases) whose stability and activity are sensitive to folding state and chaperone availability. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~70 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 50mM Tris\/HCl, pH 7.5, 0.15M NaCl and 10% glycerol\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required. For molecular chaperones, nucleotide-binding state and co-chaperone interactions often shape functional readouts.\u003c\/p\u003e\u003ch2\u003eStructural and biochemical features\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eStructural\/biochemical context:\u003c\/strong\u003e Many chaperones cycle through nucleotide-bound conformations that regulate client binding and release. Co-chaperones can tune this cycle and change apparent interaction profiles in reconstituted assays.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Changes in chaperone abundance or activity can reflect altered proteostasis demand (e.g., heat shock, oxidative stress, proteotoxic challenge) and may shift the stability landscape of client proteins. Interpreting effects often benefits from pairing chaperone measurements with client-protein stability, stress-response transcriptional markers, and aggregation\/solubility readouts.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287478125,"sku":"SPR-103A","price":275.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287510893,"sku":"SPR-103B","price":378.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-103_HSP70_Protein_SDS-Page.png?v=1770640174"},{"product_id":"hsp60-protein-bhp11900010","title":"HSP60 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP60\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSP60 (source species: Human; native localization: Mitochondrion Matrix).\u003c\/p\u003e\u003cp\u003eHuman Recombinant HSP60 Protein\u003c\/p\u003e\u003cp\u003eHSP60 is a mitochondrial chaperonin essential for the proper folding and assembly of proteins within the mitochondrial matrix. It plays a critical role in maintaining mitochondrial proteostasis, especially under conditions of cellular stress. HSP60 is highly conserved across species and is constitutively expressed, with levels increasing in response to heat shock and other stressors.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP60\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Mitochondrion Matrix\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~60 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 20mM Phosphate Buffer, 150mM NaCl, 10% glycerol\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287543661,"sku":"SPR-104A","price":194.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287576429,"sku":"SPR-104B","price":377.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-104_HSP60_Protein_SDS-Page-1.png?v=1782159108"},{"product_id":"hsc70-protein-bhp11900016","title":"HSC70 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSC70\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSC70 (source species: Human; native localization: Cytoplasm | Melanosome).\u003c\/p\u003e\u003cp\u003eHuman Recombinant HSC70 Protein\u003c\/p\u003e\u003cp\u003eHSC70 (Heat Shock Cognate 70) is a constitutively expressed member of the HSP70 family, functioning as a molecular chaperone involved in protein folding, trafficking, and degradation. Unlike its inducible counterpart HSP70, HSC70 is present under normal physiological conditions and plays a continuous role in maintaining proteostasis.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSC70\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Melanosome\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~70 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 50mM Tris\/HCl, pH8, 0.3M NaCl\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287609197,"sku":"SPR-106A","price":201.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287641965,"sku":"SPR-106B","price":287.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-106_HSC70_Protein_SDS-Page-1.png?v=1782159108"},{"product_id":"grp78-bip-protein-bhp11900019","title":"GRP78 (Bip) Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGRP78\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e GRP78 (source species: Human; native localization: Endoplasmic Reticulum Lumen | Melanosome).\u003c\/p\u003e\u003cp\u003eHuman Recombinant GRP78 (Bip) Protein\u003c\/p\u003e\u003cp\u003eGRP78, also known as BiP (Binding Immunoglobulin Protein), is a key endoplasmic reticulum (ER) chaperone involved in protein folding, quality control, and the unfolded protein response (UPR). It is a member of the HSP70 family and is upregulated during ER stress to maintain cellular homeostasis.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGRP78\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Endoplasmic Reticulum Lumen | Melanosome\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~78 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 50mM Tris\/HCl, pH 7.5, 150mM NaCl, 10% glycerol\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287674733,"sku":"SPR-107A","price":159.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287707501,"sku":"SPR-107B","price":299.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-107_GRP78_Protein_SDS-Page-1.png?v=1782159108"},{"product_id":"hsp70-protein-bhp11900022","title":"HSP70 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP70\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSP70 (source species: Human; native localization: Cytoplasm).\u003c\/p\u003e\u003cp\u003eHuman Recombinant HSP70 Full Length Protein\u003c\/p\u003e\u003cp\u003eHSP70 is a highly inducible molecular chaperone that plays a pivotal role in protein quality control across all major cellular compartments. In the brain, HSP70 is essential for preventing the aggregation of misfolded proteins, a key pathological feature of neurodegenerative diseases.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eMechanistically, \u003cstrong\u003eHSP70\u003c\/strong\u003e functions within the cellular proteostasis network, helping client proteins reach and maintain functional conformations under basal and stress conditions. Many clients are signaling proteins (e.g., kinases) whose stability and activity are sensitive to folding state and chaperone availability. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~70 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Multi-Step Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 50mM Tris\/HCl pH7.5, 2.5mM Bme, 0.15M NaCl, 10% glycerol\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required. For molecular chaperones, nucleotide-binding state and co-chaperone interactions often shape functional readouts.\u003c\/p\u003e\u003ch2\u003eStructural and biochemical features\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eStructural\/biochemical context:\u003c\/strong\u003e Many chaperones cycle through nucleotide-bound conformations that regulate client binding and release. Co-chaperones can tune this cycle and change apparent interaction profiles in reconstituted assays.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Multi-Step Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Changes in chaperone abundance or activity can reflect altered proteostasis demand (e.g., heat shock, oxidative stress, proteotoxic challenge) and may shift the stability landscape of client proteins. Interpreting effects often benefits from pairing chaperone measurements with client-protein stability, stress-response transcriptional markers, and aggregation\/solubility readouts.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287740269,"sku":"SPR-108A","price":275.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287773037,"sku":"SPR-108B","price":378.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-108_HSP70_Protein_SDS-Page-1.png?v=1782159108"},{"product_id":"hsp70-protein-bhp11900025","title":"HSP70 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP70\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSP70 (source species: Human; native localization: Cytoplasm).\u003c\/p\u003e\u003cp\u003eHuman Recombinant HSP70 Protein\u003c\/p\u003e\u003cp\u003eHSP70 is a highly inducible molecular chaperone that plays a pivotal role in protein quality control across all major cellular compartments. In the brain, HSP70 is essential for preventing the aggregation of misfolded proteins, a key pathological feature of neurodegenerative diseases.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eMechanistically, \u003cstrong\u003eHSP70\u003c\/strong\u003e functions within the cellular proteostasis network, helping client proteins reach and maintain functional conformations under basal and stress conditions. Many clients are signaling proteins (e.g., kinases) whose stability and activity are sensitive to folding state and chaperone availability. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~70 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Baculovirus\/Sf9\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified | Endotoxin-free\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 50mM Tris\/HCl, pH 7.5, 0.15M NaCl, 10% glycerol\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Insect-cell expression supports eukaryotic folding and some PTMs, which can be beneficial for structurally complex proteins. Glycan patterns may differ from mammalian cells and can influence certain binding-dependent assays. For molecular chaperones, nucleotide-binding state and co-chaperone interactions often shape functional readouts.\u003c\/p\u003e\u003ch2\u003eStructural and biochemical features\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eStructural\/biochemical context:\u003c\/strong\u003e Many chaperones cycle through nucleotide-bound conformations that regulate client binding and release. Co-chaperones can tune this cycle and change apparent interaction profiles in reconstituted assays.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Baculovirus\/Sf9. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified | Endotoxin-free. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Changes in chaperone abundance or activity can reflect altered proteostasis demand (e.g., heat shock, oxidative stress, proteotoxic challenge) and may shift the stability landscape of client proteins. Interpreting effects often benefits from pairing chaperone measurements with client-protein stability, stress-response transcriptional markers, and aggregation\/solubility readouts.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287805805,"sku":"SPR-115A","price":328.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287838573,"sku":"SPR-115B","price":481.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-115_HSP70_Protein_SDS-Page.png?v=1770640176"},{"product_id":"hsp65-protein-bhp11900028","title":"HSP65 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP65\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSP65 (source species: Bacteria; native localization: Cytoplasm).\u003c\/p\u003e\u003cp\u003eMycobacterium bovis BCG Recombinant HSP65 Protein\u003c\/p\u003e\u003cp\u003eHSP65, a member of the HSP60 family, is a mitochondrial chaperonin originally identified in Mycobacterium bovis BCG. It shares high sequence homology with HSP60 proteins across species and plays a central role in protein folding, particularly in the mitochondrial matrix. Like other chaperonins, HSP65 assists in the ATP-dependent folding and assembly of polypeptides, ensuring proper protein conformation and cellular function.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP65\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Bacteria\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~65 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Multi-Step Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 20mM Tris\/HCl, pH 7.5, 0.45M NaCl, 10% glycerol, 5mM bMe\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Multi-Step Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287871341,"sku":"SPR-116A","price":246.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287904109,"sku":"SPR-116B","price":348.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-116_HSP65_Protein_SDS-Page.png?v=1770640176"},{"product_id":"hsp70-protein-bhp11900031","title":"HSP70 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP70\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSP70 (source species: Human; native localization: Cytoplasm).\u003c\/p\u003e\u003cp\u003eHuman Recombinant HSP70 Full Length Protein\u003c\/p\u003e\u003cp\u003eHSP70 is a highly inducible molecular chaperone that plays a pivotal role in protein quality control across all major cellular compartments. In the brain, HSP70 is essential for preventing the aggregation of misfolded proteins, a key pathological feature of neurodegenerative diseases.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eMechanistically, \u003cstrong\u003eHSP70\u003c\/strong\u003e functions within the cellular proteostasis network, helping client proteins reach and maintain functional conformations under basal and stress conditions. Many clients are signaling proteins (e.g., kinases) whose stability and activity are sensitive to folding state and chaperone availability. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~70 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Baculovirus\/Sf9\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Multi-Step Purified | Endotoxin-free\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 50mM Tris\/HCl pH7.5, 0.3M NaCl, 10% glycerol, 0.1mM EDTA\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Insect-cell expression supports eukaryotic folding and some PTMs, which can be beneficial for structurally complex proteins. Glycan patterns may differ from mammalian cells and can influence certain binding-dependent assays. For molecular chaperones, nucleotide-binding state and co-chaperone interactions often shape functional readouts.\u003c\/p\u003e\u003ch2\u003eStructural and biochemical features\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eStructural\/biochemical context:\u003c\/strong\u003e Many chaperones cycle through nucleotide-bound conformations that regulate client binding and release. Co-chaperones can tune this cycle and change apparent interaction profiles in reconstituted assays.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Baculovirus\/Sf9. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Multi-Step Purified | Endotoxin-free. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Changes in chaperone abundance or activity can reflect altered proteostasis demand (e.g., heat shock, oxidative stress, proteotoxic challenge) and may shift the stability landscape of client proteins. Interpreting effects often benefits from pairing chaperone measurements with client-protein stability, stress-response transcriptional markers, and aggregation\/solubility readouts.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016287936877,"sku":"SPR-117A","price":352.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016287969645,"sku":"SPR-117B","price":528.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-117_HSP70_Protein_SDS-Page.png?v=1770640176"},{"product_id":"grp78-bip-protein-bhp11900037","title":"GRP78 (Bip) Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGRP78\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e GRP78 (source species: Human; native localization: Endoplasmic Reticulum Lumen | Melanosome).\u003c\/p\u003e\u003cp\u003eHuman Recombinant GRP78 (Bip) Full Length Protein\u003c\/p\u003e\u003cp\u003eGRP78, also known as BiP (Binding Immunoglobulin Protein), is a key endoplasmic reticulum (ER) chaperone involved in protein folding, quality control, and the unfolded protein response (UPR). It is a member of the HSP70 family and is upregulated during ER stress to maintain cellular homeostasis.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGRP78\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Endoplasmic Reticulum Lumen | Melanosome\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~78 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 20mM Tris\/HCl pH7.5, 50mM KCl, 5mM MgCl2, 1mM DTT\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288002413,"sku":"SPR-119A","price":183.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016288035181,"sku":"SPR-119B","price":337.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-119_GRP78_Protein_SDS-Page.png?v=1770640177"},{"product_id":"rab5-protein-bhp11900040","title":"Rab5 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eRAB5\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e RAB5 (source species: Human; native localization: Cell Membrane | Early Endosome Membrane | Melanosome).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Rab5 Protein\u003c\/p\u003e\u003cp\u003eRab5 is a small GTPase of the Ras superfamily that plays a central role in regulating early endocytic trafficking. It cycles between an inactive GDP-bound state and an active GTP-bound state, a process tightly controlled by regulatory proteins such as GEFs, GAPs, and GDIs. In its active form, Rab5 associates with early endosomal membranes, where it recruits effector proteins like EEA1 and Rabaptin-5 to mediate vesicle docking, fusion, and cargo sorting.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eRAB5\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cell Membrane | Early Endosome Membrane | Melanosome\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~26 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 20mM Tris\/HCl pH7.5, 0.45M NaCl, 10% glycerol, 0.5mM DTT\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288067949,"sku":"SPR-121A","price":477.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016288100717,"sku":"SPR-121B","price":884.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-121_RAB5_Protein_SDS-Page.png?v=1770640177"},{"product_id":"hsp90-protein-bhp11900043","title":"HSP90 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP90\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HSP90 (source species: P. falciparum; native localization: Cytoplasm | Melanosome).\u003c\/p\u003e\u003cp\u003eP. Falciparum Recombinant HSP90 Partial Protein\u003c\/p\u003e\u003cp\u003eHSP90 is a highly conserved and abundantly expressed molecular chaperone that exists in two major cytosolic isoforms: HSP90α and HSP90β. It is essential for the folding, stabilization, and functional regulation of a wide array of client proteins, many of which are involved in signal transduction, cell cycle control, and stress responses.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eMechanistically, \u003cstrong\u003eHSP90\u003c\/strong\u003e functions within the cellular proteostasis network, helping client proteins reach and maintain functional conformations under basal and stress conditions. Many clients are signaling proteins (e.g., kinases) whose stability and activity are sensitive to folding state and chaperone availability. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e P. falciparum\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Melanosome\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Partial\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~21.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 50mM Tris\/HCl pH7.5, 300mM NaCl, 10% glycerol\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required. For molecular chaperones, nucleotide-binding state and co-chaperone interactions often shape functional readouts.\u003c\/p\u003e\u003ch2\u003eStructural and biochemical features\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eStructural\/biochemical context:\u003c\/strong\u003e Many chaperones cycle through nucleotide-bound conformations that regulate client binding and release. Co-chaperones can tune this cycle and change apparent interaction profiles in reconstituted assays.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Changes in chaperone abundance or activity can reflect altered proteostasis demand (e.g., heat shock, oxidative stress, proteotoxic challenge) and may shift the stability landscape of client proteins. Interpreting effects often benefits from pairing chaperone measurements with client-protein stability, stress-response transcriptional markers, and aggregation\/solubility readouts.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288133485,"sku":"SPR-122A","price":183.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016288166253,"sku":"SPR-122B","price":306.0,"currency_code":"USD","in_stock":true}]},{"product_id":"l-citrulline-bsa-conjugate-bhp11900052","title":"MOLECULAR SIGNATURE® L-Citrulline BSA Conjugate","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eL-Citrulline\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003eL-Citrulline conjugated to Bovine Serum Albumin (BSA)\u003c\/p\u003e\u003cp\u003eL-Citrulline BSA Conjugate is a specialized biochemical tool used to investigate protein citrullination, a post-translational modification where peptidyl-arginine is converted to peptidyl-citrulline. This process, catalyzed by peptidylarginine deiminases (PADs), alters protein structure and function, influencing cellular signaling and immune responses.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eL-Citrulline\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCell Signaling\u003c\/strong\u003e and \u003cstrong\u003ePost-translational Modifications\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Filter Sterilized (0.2 µm)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4, 0.09% Sodium Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Expression host can influence folding and PTMs (e.g., glycosylation, disulfide bonds), which may impact stability or binding depending on protein class.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Filter Sterilized (0.2 µm). Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288199021,"sku":"SPR-200A","price":223.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-200_L-Citrulline-BSA-Conjugate-Protein-Western-Blot-1.png?v=1770640177"},{"product_id":"n-acetylglucosamine-bsa-glycoconjugate-bhp11900055","title":"MOLECULAR SIGNATURE® N-Acetylglucosamine BSA Glycoconjugate","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eN-Acetylglucosamine\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003eGlycated Bovine Serum Albumin (BSA) with β-N-Acetylglucosamine\u003c\/p\u003e\u003cp\u003eN-Acetylglucosamine (GlcNAc) BSA Glycoconjugate is a powerful molecular probe for studying glycosylation-dependent signaling in the nervous system. GlcNAc is a key monosaccharide involved in N-glycan branching, a process critical for modulating receptor clustering, endocytosis, and immune regulation.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eN-Acetylglucosamine\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCell Signaling\u003c\/strong\u003e and \u003cstrong\u003ePost-translational Modifications\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Filter Sterilized (0.2 µm)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4, 0.09% Sodium Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Expression host can influence folding and PTMs (e.g., glycosylation, disulfide bonds), which may impact stability or binding depending on protein class.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Filter Sterilized (0.2 µm). Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288231789,"sku":"SPR-201A","price":223.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-201_N-Acetylglucosamine-BSA-Glycoconjugate-Protein-Western-Blot-1.png?v=1770640178"},{"product_id":"n-acetylgalactosamine-bsa-glycoconjugate-bhp11900058","title":"MOLECULAR SIGNATURE® N-Acetylgalactosamine BSA Glycoconjugate","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eN-Acetylgalactosamine\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003eGlycated Bovine Serum Albumin (BSA) with α-N-Acetylgalactosamine\u003c\/p\u003e\u003cp\u003eN-Acetylgalactosamine (GalNAc) BSA Glycoconjugate is a synthetic glycoprotein mimic used to study O-linked glycosylation in the central nervous system. GalNAc is the initiating sugar in mucin-type O-glycans, which regulate protein stability, trafficking, and cell-cell communication.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eN-Acetylgalactosamine\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCell Signaling\u003c\/strong\u003e and \u003cstrong\u003ePost-translational Modifications\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Filter Sterilized (0.2 µm)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4, 0.09% Sodium Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Expression host can influence folding and PTMs (e.g., glycosylation, disulfide bonds), which may impact stability or binding depending on protein class.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Filter Sterilized (0.2 µm). Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288264557,"sku":"SPR-202A","price":287.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-202_N-Acetylgalactosamine-BSA-Glycoconjugate-Protein-Western-Blot-1.png?v=1770640178"},{"product_id":"hexanoyl-lysine-adduct-bsa-conjugate-bhp11900067","title":"MOLECULAR SIGNATURE® Hexanoyl-Lysine adduct BSA Conjugate","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHexanoyl-Lysine adduct\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003eBovine Serum Albumin (BSA) modified with Hexanoyl-Lysine adduct (HEL)\u003c\/p\u003e\u003cp\u003eHexanoyl-Lysine Adduct (HEL) BSA Conjugate is a lipid peroxidation biomarker used to detect early oxidative stress in neural tissues. HEL forms when omega-6 polyunsaturated fatty acids undergo peroxidation, generating reactive aldehydes that covalently modify lysine residues on proteins.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHexanoyl-Lysine adduct\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eOxidative Stress\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Filter Sterilized (0.2 µm)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4, 0.09% Sodium Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Expression host can influence folding and PTMs (e.g., glycosylation, disulfide bonds), which may impact stability or binding depending on protein class.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Filter Sterilized (0.2 µm). Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288297325,"sku":"SPR-205A","price":287.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-205_Hexanoyl-Lysine-adduct-BSA-Conjugate-Protein-Western-Blot-1.png?v=1770640178"},{"product_id":"acrolein-bsa-conjugate-bhp11900070","title":"MOLECULAR SIGNATURE® Acrolein BSA Conjugate","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAcrolein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003eBovine Serum Albumin (BSA) modified with Acrolein\u003c\/p\u003e\u003cp\u003eAcrolein BSA Conjugate is a critical tool for detecting acrolein-modified proteins, which serve as biomarkers of oxidative stress and lipid peroxidation in the nervous system. Acrolein, a highly reactive α,β-unsaturated aldehyde, is generated during lipid degradation and inflammation, particularly under conditions of mitochondrial dysfunction and excitotoxicity.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAcrolein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eOxidative Stress\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Filter Sterilized (0.2 µm)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4, 0.09% Sodium Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Expression host can influence folding and PTMs (e.g., glycosylation, disulfide bonds), which may impact stability or binding depending on protein class.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Filter Sterilized (0.2 µm). Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288330093,"sku":"SPR-206A","price":223.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-206_Acrolein-BSA-Conjugate-Protein-Western-Blot-1.png?v=1770640178"},{"product_id":"crotonaldehyde-bsa-conjugate-bhp11900073","title":"MOLECULAR SIGNATURE® Crotonaldehyde BSA Conjugate","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCrotonaldehyde\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003eBovine Serum Albumin (BSA) modified with Crotonaldehyde\u003c\/p\u003e\u003cp\u003eCrotonaldehyde BSA Conjugate is used to study the impact of lipid peroxidation-derived aldehydes on neural function. Crotonaldehyde, a byproduct of oxidative stress and environmental exposure, forms stable adducts with lysine residues, altering protein structure and function.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCrotonaldehyde\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eOxidative Stress\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Filter Sterilized (0.2 µm)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4, 0.09% Sodium Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Expression host can influence folding and PTMs (e.g., glycosylation, disulfide bonds), which may impact stability or binding depending on protein class.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Filter Sterilized (0.2 µm). Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288362861,"sku":"SPR-207A","price":287.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-207_Crotonaldehyde-BSA-Conjugate-Protein-Western-Blot-1.png?v=1770640179"},{"product_id":"malondialdehyde-bsa-conjugate-bhp11900079","title":"MOLECULAR SIGNATURE® Malondialdehyde BSA Conjugate","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMalondialdehyde\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003eBovine Serum Albumin (BSA) modified with Malondialdehyde\u003c\/p\u003e\u003cp\u003eMalondialdehyde (MDA) BSA Conjugate is a well-established marker of lipid peroxidation and oxidative stress in neural tissues. MDA is generated during polyunsaturated fatty acid degradation and forms covalent adducts with proteins, altering their function and immunogenicity.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMalondialdehyde\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eOxidative Stress\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Filter Sterilized (0.2 µm)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4, 0.09% Sodium Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Expression host can influence folding and PTMs (e.g., glycosylation, disulfide bonds), which may impact stability or binding depending on protein class.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Filter Sterilized (0.2 µm). Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288395629,"sku":"SPR-209A","price":223.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-209_Malondialdehyde-BSA-Conjugate-Protein-Western-Blot-1.png?v=1770640179"},{"product_id":"4-hydroxy-2-hexenal-bsa-conjugate-bhp11900082","title":"MOLECULAR SIGNATURE® 4-Hydroxy-2-hexenal BSA Conjugate","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003e4-Hydroxy-2-hexenal\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003eBovine Serum Albumin (BSA) modified with 4-Hydroxy-2-hexenal (4-HHE)\u003c\/p\u003e\u003cp\u003e4-Hydroxy-2-hexenal (HHE) BSA Conjugate is a lipid peroxidation marker used to study oxidative damage in neural tissues. HHE is generated from the oxidation of omega-3 polyunsaturated fatty acids and forms covalent adducts with proteins, altering their structure and function.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003e4-Hydroxy-2-hexenal\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eOxidative Stress\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Filter Sterilized (0.2 µm)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4, 0.09% Sodium Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Expression host can influence folding and PTMs (e.g., glycosylation, disulfide bonds), which may impact stability or binding depending on protein class.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Filter Sterilized (0.2 µm). Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288428397,"sku":"SPR-210A","price":287.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-210_4-Hydroxy-2-hexenal-BSA-Conjugate-Protein-Western-Blot-1.png?v=1770640179"},{"product_id":"4-hydroxynonenal-bsa-conjugate-bhp11900085","title":"MOLECULAR SIGNATURE® 4-Hydroxynonenal BSA Conjugate","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003e4-Hydroxynonenal\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003eBovine Serum Albumin (BSA) modified with 4-Hydroxy nonenal (4-HNE)\u003c\/p\u003e\u003cp\u003e4-Hydroxynonenal (4-HNE) BSA Conjugate is a widely used biomarker for lipid peroxidation and oxidative stress in the brain. 4-HNE is derived from omega-6 fatty acid oxidation and forms stable adducts with nucleophilic amino acids, disrupting protein function and cellular signaling.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003e4-Hydroxynonenal\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eOxidative Stress\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Filter Sterilized (0.2 µm)\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4, 0.09% Sodium Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Expression host can influence folding and PTMs (e.g., glycosylation, disulfide bonds), which may impact stability or binding depending on protein class.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e Synthetic. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Filter Sterilized (0.2 µm). Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288461165,"sku":"SPR-211A","price":223.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-211_4-Hydroxynonenal-BSA-Conjugate-Protein-Western-Blot-1.png?v=1770640180"},{"product_id":"aha1-protein-bhp11900091","title":"AHA1 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAHA1\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e AHA1 (source species: Human; native localization: Cytoplasm).\u003c\/p\u003e\u003cp\u003eHuman Recombinant AHA1 Protein\u003c\/p\u003e\u003cp\u003eAHA1 (Activator of HSP90 ATPase 1) is a co-chaperone that enhances the ATPase activity of HSP90, accelerating its chaperone cycle and modulating the folding of client proteins. In the nervous system, AHA1 plays a critical role in regulating the stability and function of proteins involved in synaptic signaling, neuronal development, and stress responses.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAHA1\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~38 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Multi-Step Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Multi-Step Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288493933,"sku":"SPR-300A","price":231.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016288526701,"sku":"SPR-300B","price":365.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-300_AHA1_Protein_SDS-Page.png?v=1770640180"},{"product_id":"hop-protein-bhp11900094","title":"HOP Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHOP\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HOP (source species: Human; native localization: Cytoplasm | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant HOP Protein\u003c\/p\u003e\u003cp\u003eHOP (HSP70-HSP90 Organizing Protein) is a co-chaperone that facilitates the transfer of client proteins between HSP70 and HSP90, coordinating their folding and maturation. It acts as a scaffold, linking the two chaperone systems and ensuring efficient proteostasis under both normal and stress conditions.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHOP\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~63 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 25mM HEPES pH 7.2, 50mM NaCl, 1mM DTT, 10% glycerol\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAffinity tag (sequence-indicated):\u003c\/strong\u003e His-tag\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e The provided sequence suggests a \u003cstrong\u003eHis-tag\u003c\/strong\u003e, which can simplify capture\/immobilization workflows in binding assays. Tag status can also influence complex formation in some contexts.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288559469,"sku":"SPR-302A","price":183.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016288592237,"sku":"SPR-302B","price":306.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-302_HOP_Protein_SDS-Page.png?v=1770640180"},{"product_id":"p23-protein-bhp11900097","title":"p23 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eP23\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e P23 (source species: Human; native localization: Cytoplasm).\u003c\/p\u003e\u003cp\u003eHuman Recombinant p23 Protein\u003c\/p\u003e\u003cp\u003ep23 is a small co-chaperone that stabilizes the ATP-bound conformation of HSP90, promoting the maturation of client proteins and preventing premature release. It plays a key role in the late stages of the HSP90 chaperone cycle, ensuring proper folding and functional activation of a wide range of signaling proteins.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eP23\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eHeat Shock\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~23 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"50 ug","offer_id":53016288625005,"sku":"SPR-303A","price":231.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53016288657773,"sku":"SPR-303B","price":365.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-303_p23_Protein_SDS-Page.png?v=1770640181"},{"product_id":"alpha-synuclein-monomers-bhp11900124","title":"Alpha Synuclein Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Alpha Synuclein Monomers (Type 2)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016288690541,"sku":"SPR-316B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016288723309,"sku":"SPR-316C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016288756077,"sku":"SPR-316E","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-316_Alpha-Synuclein-Protein-Monomer-Protein-SDS-Page-1.png?v=1770644811"},{"product_id":"alpha-synuclein-pre-formed-fibrils-bhp11900127","title":"Alpha Synuclein Pre-formed Fibrils","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Alpha Synuclein PFFs (Type 2)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016288788845,"sku":"SPR-317B","price":390.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016288821613,"sku":"SPR-317C","price":700.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016288854381,"sku":"SPR-317E","price":1455.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-317_Alpha-Synuclein-Preformed-Fibrils-Protein-TEM-4.png?v=1782159109"},{"product_id":"alpha-synuclein-monomers-bhp11900139","title":"Alpha Synuclein Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Alpha Synuclein Monomers (Type 1)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016288887149,"sku":"SPR-321B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016288919917,"sku":"SPR-321C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016288952685,"sku":"SPR-321E","price":1435.0,"currency_code":"USD","in_stock":true},{"title":"500 ug (@5 mg\/ml)","offer_id":53016288985453,"sku":"SPR-321XE","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-321_Alpha-Synuclein-Protein-Monomer-Thioflavin-T-assay-1.png?v=1770644812"},{"product_id":"alpha-synuclein-pre-formed-fibrils-bhp11900142","title":"Alpha Synuclein Pre-formed Fibrils","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Alpha Synuclein PFFs (Type 1)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. 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Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016289018221,"sku":"SPR-322B","price":390.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016289050989,"sku":"SPR-322C","price":700.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016289083757,"sku":"SPR-322E","price":1455.0,"currency_code":"USD","in_stock":true},{"title":"500 ug (@5 mg\/ml)","offer_id":53016289116525,"sku":"SPR-322XE","price":1455.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-322_Alpha-Synuclein-Protein-Preformed-Fibrils-Protein-TEM-7.png?v=1782159109"},{"product_id":"alpha-synuclein-monomers-bhp11900145","title":"Alpha Synuclein Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Mouse; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eMouse Recombinant Alpha Synuclein Monomers (Type 1)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. 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Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016289149293,"sku":"SPR-323B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016289182061,"sku":"SPR-323C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016289214829,"sku":"SPR-323E","price":1435.0,"currency_code":"USD","in_stock":true},{"title":"500 ug (@5 mg\/ml)","offer_id":53016289247597,"sku":"SPR-323XE","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-323_Alpha-Synuclein-Protein-IHC-1.png?v=1770644813"},{"product_id":"alpha-synuclein-pre-formed-fibrils-bhp11900148","title":"Alpha Synuclein Pre-formed Fibrils","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Mouse; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eMouse Recombinant Alpha Synuclein PFFs (Type 1)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016289378669,"sku":"SPR-324B","price":390.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016289411437,"sku":"SPR-324C","price":700.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016289444205,"sku":"SPR-324E","price":1455.0,"currency_code":"USD","in_stock":true},{"title":"500 ug (@5 mg\/ml)","offer_id":53016289476973,"sku":"SPR-324XE","price":1455.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-324_Alpha-Synuclein-Protein-Preformed-Fibrils-ICC-IF-1.png?v=1782159109"},{"product_id":"tau-441-2n4r-p301s-mutant-monomers-bhp11900151","title":"Tau-441 (2N4R) P301S Mutant Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Tau (source species: Human; native localization: Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Tau-441 (2N4R) P301S Mutant Monomers\u003c\/p\u003e\u003cp\u003eAlzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing hyperphosphorylated tau fibrils (3). There are six isoforms of tau in the adult human brain: three with four repeat units (4R) and three with three repeat units (3R) (4). 2N4R, or Tau-441 is the full length tau protein. P301S is a mutation encoded by exon 10 (4) that impairs the ability of tau to assemble microtubules (5).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eAlzheimer's Disease\u003c\/strong\u003e and \u003cstrong\u003eAxon Markers\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~45.8 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 10 mM HEPES, 100 mM NaCl pH 7.4\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAffinity tag (sequence-indicated):\u003c\/strong\u003e GST-tag\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e The provided sequence suggests a \u003cstrong\u003eGST-tag\u003c\/strong\u003e, which can simplify capture\/immobilization workflows in binding assays. Tag status can also influence complex formation in some contexts.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016289509741,"sku":"SPR-327B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016289542509,"sku":"SPR-327C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016289575277,"sku":"SPR-327E","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-327_Tau-Protein-Monomer-SDS-PAGE-1.png?v=1770644813"},{"product_id":"tau-k18-p301l-mutant-monomers-bhp11900154","title":"Tau (K18) P301L Mutant Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Tau (source species: Human; native localization: Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Tau (K18) P301L Mutant Monomers\u003c\/p\u003e\u003cp\u003eAlzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing hyperphosphorylated tau fibrils (3). There are six isoforms of tau in the adult human brain: three with four repeat units (4R) and three with three repeat units (3R) (4). K18 is a truncated form of human tau containing only the 4 microtubule binding repeats (5). P301L (PL) is a mutation where proline is replaced by leucine at codon 301 of tau, and has been linked to frontotemporal dementia (6).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eAlzheimer's Disease\u003c\/strong\u003e and \u003cstrong\u003eAxon Markers\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Partial\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~15.1 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 10 mM HEPES, 100 mM NaCl pH 7.4\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAffinity tag (sequence-indicated):\u003c\/strong\u003e GST-tag\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e The provided sequence suggests a \u003cstrong\u003eGST-tag\u003c\/strong\u003e, which can simplify capture\/immobilization workflows in binding assays. Tag status can also influence complex formation in some contexts.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016289608045,"sku":"SPR-328B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016289640813,"sku":"SPR-328C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016289673581,"sku":"SPR-328E","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-328_Tau-Protein-Monomer-SDS-PAGE-1.png?v=1770644814"},{"product_id":"tau-441-2n4r-p301s-mutant-pre-formed-fibrils-bhp11900157","title":"Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Tau (source species: Human; native localization: Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Tau-441 (2N4R) P301S Mutant PFFs\u003c\/p\u003e\u003cp\u003eAlzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing hyperphosphorylated tau fibrils (3). There are six isoforms of tau in the adult human brain: three with four repeat units (4R) and three with three repeat units (3R) (4). 2N4R, or Tau-441 is the full length tau protein. P301S is a mutation encoded by exon 10 (4) that impairs the ability of tau to assemble microtubules (5).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eAlzheimer's Disease\u003c\/strong\u003e and \u003cstrong\u003eAxon Markers\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~45.8 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 10 mM HEPES, 100 mM NaCl pH 7.4\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAffinity tag (sequence-indicated):\u003c\/strong\u003e GST-tag\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e The provided sequence suggests a \u003cstrong\u003eGST-tag\u003c\/strong\u003e, which can simplify capture\/immobilization workflows in binding assays. Tag status can also influence complex formation in some contexts.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016289706349,"sku":"SPR-329B","price":390.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016289739117,"sku":"SPR-329C","price":700.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016289771885,"sku":"SPR-329E","price":1455.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-329_Tau-Protein-Peformed-Fibrils-TEM-1.png?v=1770644814"},{"product_id":"tau-k18-p301l-mutant-pre-formed-fibrils-bhp11900160","title":"Tau (K18) P301L Mutant Pre-formed Fibrils","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Tau (source species: Human; native localization: Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Tau (K18) P301L Mutant PFFs\u003c\/p\u003e\u003cp\u003eAlzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing hyperphosphorylated tau fibrils (3). There are six isoforms of tau in the adult human brain: three with four repeat units (4R) and three with three repeat units (3R) (4). K18 is a truncated form of human tau containing only the 4 microtubule binding repeats (5). P301L (PL) is a mutation where proline is replaced by leucine at codon 301 of tau, and has been linked to frontotemporal dementia (6).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eAlzheimer's Disease\u003c\/strong\u003e and \u003cstrong\u003eAxon Markers\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Partial\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~15.1 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 10 mM HEPES, 100 mM NaCl pH 7.4\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAffinity tag (sequence-indicated):\u003c\/strong\u003e GST-tag\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e The provided sequence suggests a \u003cstrong\u003eGST-tag\u003c\/strong\u003e, which can simplify capture\/immobilization workflows in binding assays. Tag status can also influence complex formation in some contexts.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016289804653,"sku":"SPR-330B","price":390.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016289837421,"sku":"SPR-330C","price":700.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016289870189,"sku":"SPR-330E","price":1455.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-330_Tau-Protein-Preformed-Fibrils-TEM-1.png?v=1770644815"},{"product_id":"alpha-synuclein-a53t-mutant-monomers-bhp11900163","title":"Alpha Synuclein A53T Mutant Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Alpha Synuclein A53T Mutant Monomers (Type 1)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6). The A53T mutation is a missense point mutation where alanine is replaced by threonine at the 53rd amino acid. This mutation has been linked to early-onset Parkinson's Disease and increased rates of alpha synuclein fibrillization.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016289902957,"sku":"SPR-325B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016289935725,"sku":"SPR-325C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016289968493,"sku":"SPR-325E","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-325_A53T-Alpha-Synuclein-Monomer-Protein-SDS-PAGE-1.png?v=1770644815"},{"product_id":"alpha-synuclein-a53t-mutant-pre-formed-fibrils-bhp11900164","title":"Alpha Synuclein A53T Mutant Pre-formed Fibrils","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Alpha Synuclein A53T Mutant PFFs (Type 1)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6). The A53T mutation is a missense point mutation where alanine is replaced by threonine at the 53rd amino acid. This mutation has been linked to early-onset Parkinson's Disease (7) and increased rates of alpha synuclein fibrillization (8).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290001261,"sku":"SPR-326B","price":390.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290034029,"sku":"SPR-326C","price":700.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290066797,"sku":"SPR-326E","price":1455.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-326_A53T-Alpha-Synuclein-Preformed-Fibrils-Protein-TEM-2.png?v=1782159109"},{"product_id":"alpha-synuclein-pre-formed-fibrils-atto-594-bhp11901098","title":"Alpha Synuclein Pre-formed Fibrils: ATTO 594","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Alpha Synuclein PFFs: ATTO 594 (Type 1)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH7.4, 0.09% Azide\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290099565,"sku":"SPR-322B-A594","price":440.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290132333,"sku":"SPR-322C-A594","price":790.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290165101,"sku":"SPR-322E-A594","price":1640.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-322-A594_Alpha-Synuclein-Protein-Protein-TEM-1.png?v=1770644815"},{"product_id":"tau-441-2n4r-p301s-mutant-pre-formed-fibrils-atto-488-bhp11901115","title":"Tau-441 (2N4R) P301S Mutant Pre-formed Fibrils: ATTO 488","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Tau (source species: Human; native localization: Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Tau-441 (2N4R) P301S Mutant PFFs: ATTO 488\u003c\/p\u003e\u003cp\u003eAlzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing hyperphosphorylated tau fibrils (3). There are six isoforms of tau in the adult human brain: three with four repeat units (4R) and three with three repeat units (3R) (4). 2N4R, or Tau-441 is the full length tau protein. P301S is a mutation encoded by exon 10 (4) that impairs the ability of tau to assemble microtubules (5).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eAlzheimer's Disease\u003c\/strong\u003e and \u003cstrong\u003eAxon Markers\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH7.4, 0.09% Azide\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAffinity tag (sequence-indicated):\u003c\/strong\u003e GST-tag\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e The provided sequence suggests a \u003cstrong\u003eGST-tag\u003c\/strong\u003e, which can simplify capture\/immobilization workflows in binding assays. Tag status can also influence complex formation in some contexts.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290197869,"sku":"SPR-329B-A488","price":440.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290230637,"sku":"SPR-329C-A488","price":790.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290263405,"sku":"SPR-329E-A488","price":1640.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-329-A488_Tau-Protein-Protein-TEM-1.png?v=1770644816"},{"product_id":"alpha-synuclein-n-terminal-acetylated-monomers-bhp11901120","title":"Alpha Synuclein N-Terminal Acetylated Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant N-Terminal Acetylated Alpha Synuclein Monomers (Type 1)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6). Alpha synuclein purified from both normal and pathological brain tissue is N-acetylated (7) and this post-translational modification affects affect alpha-synuclein stability and toxicity (8).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290296173,"sku":"SPR-331B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290328941,"sku":"SPR-331C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290361709,"sku":"SPR-331E","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-331_N-Terminal-Acetylated-Alpha-Synuclein-Monomer-Protein-Western-Blot-1.png?v=1770644816"},{"product_id":"alpha-synuclein-n-terminal-acetylated-pre-formed-fibrils-bhp11901123","title":"Alpha Synuclein N-Terminal Acetylated Pre-formed Fibrils","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant N-Terminal Acetylated Alpha Synuclein PFFs (Type 1)\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6). Alpha synuclein purified from both normal and pathological brain tissue is N-acetylated (7) and this post-translational modification affects affect alpha-synuclein stability and toxicity (8).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full Length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290394477,"sku":"SPR-332B","price":390.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290427245,"sku":"SPR-332C","price":700.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290460013,"sku":"SPR-332E","price":1455.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-332_N-Terminal-Acetylated-Alpha-Synuclein-Fibril-Protein-TEM-1.png?v=1770644819"},{"product_id":"beta-synuclein-monomers-bhp11901126","title":"Beta Synuclein Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBeta-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Beta-synuclein (source species: Human; native localization: Cytoplasm).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Beta Synuclein Monomers\u003c\/p\u003e\u003cp\u003eAlzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). Beta synuclein is suggested to be an inhibitor of alpha synuclein aggregation- protecting the central nervous system from the neurotoxin effects of alpha synuclein (3).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBeta-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 14.28 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290492781,"sku":"SPR-405B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290525549,"sku":"SPR-405C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290558317,"sku":"SPR-405E","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-405_Beta-Synuclein-Protein-Protein-Thioflavin-T-assay-1.png?v=1770644817"},{"product_id":"gamma-synuclein-monomers-bhp11901132","title":"Gamma Synuclein Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGamma-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Gamma-synuclein (source species: Human; native localization: Cytoskeleton | Centrosome | Spindle | Perinuclear Region).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Gamma Synuclein Monomers\u003c\/p\u003e\u003cp\u003eGamma synuclein is a neuronal protein found in peripheral and motor nerve systems. It has been implicated in the hippocampal axon pathology in Parkinson's Disease (1). Its expression in breast tumors is also a marker for tumor progression (3).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGamma-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoskeleton | Centrosome | Spindle | Perinuclear Region\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 13.33 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. 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Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290591085,"sku":"SPR-407B","price":430.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290623853,"sku":"SPR-407C","price":770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290656621,"sku":"SPR-407E","price":1605.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-407_Gamma-Synuclein-Monomer-Protein-Thioflavin-T-assay-1.png?v=1770644817"},{"product_id":"sod1-monomers-bhp11901138","title":"SOD1 Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSOD1\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e SOD1 (source species: Human; native localization: Nucleus | Mitochondrion | Cytoplasm).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Superoxide Dismutase 1 (SOD1) Monomers\u003c\/p\u003e\u003cp\u003eSuperoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2ˉ to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2,5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extra-cellular space (7). SOD3 can also be distinguished by its heparin-binding capacity (1). Studies have shown that in vitro, Cu-Zn SOD (SOD1) fibrils are transduced into cells and function as seeds to trigger the aggregation of endogenously expressed SOD1 (9).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSOD1\u003c\/strong\u003e is often examined as part of cellular redox homeostasis, buffering reactive oxygen species and shaping redox-sensitive signaling. Because oxidative cues can alter protein function and transcriptional responses, redox regulators are widely used as mechanistic probes in stress biology. This protein is frequently discussed in research themes such as \u003cstrong\u003eCancer\u003c\/strong\u003e and \u003cstrong\u003eOxidative Stress\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Nucleus | Mitochondrion | Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 15.936 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PB pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290689389,"sku":"SPR-435B","price":430.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290722157,"sku":"SPR-435C","price":770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290754925,"sku":"SPR-435E","price":1605.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-435_SOD1-Protein-SDS-PAGE-1.png?v=1770644818"},{"product_id":"tau-dgae-297-391-monomers-bhp11901141","title":"Tau dGAE (297-391) Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Tau (source species: Human; native localization: Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Tau dGAE (297-391) Monomers\u003c\/p\u003e\u003cp\u003eAlzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing paired helical filaments (PHFs). A truncated 95-amino acid fragment corresponding to residues 297-391 of full-length tau has been shown to assemble into PHF-like fibrils in vitro in the absence of additives or templates (3). This fragment has been found in the core of PHFs from AD brains and forms filaments that closely resemble PHFs isolated from AD brains (3).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eAlzheimer's Disease\u003c\/strong\u003e and \u003cstrong\u003eAxon Markers\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Fragment\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 10.165 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PB pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290787693,"sku":"SPR-444B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290820461,"sku":"SPR-444C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290853229,"sku":"SPR-444E","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-444_Tau-Protein-Monomer-Protein-Thioflavin-T-assay-1.png?v=1770644818"},{"product_id":"tau-dgae-297-391-c322a-mutant-monomers-bhp11901144","title":"Tau dGAE (297-391) C322A Mutant Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Tau (source species: Human; native localization: Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Tau dGAE (297-391) C322A Mutant Monomers\u003c\/p\u003e\u003cp\u003eAlzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing paired helical filaments (PHFs). A truncated 95-amino acid fragment corresponding to residues 297-391 of full-length tau has been shown to assemble into PHF-like fibrils in vitro in the absence of additives or templates (3). This fragment has been found in the core of PHFs from AD brains and forms filaments that closely resemble PHFs isolated from AD brains (3). The C322A mutation leads to enhanced self-assembly into long and ordered PHFs (3).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTau\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eAlzheimer's Disease\u003c\/strong\u003e and \u003cstrong\u003eAxon Markers\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Axolemma | Axolemma Plasma Membrane | Axon | Cell Body | Cell membrane | Cytoplasmic Ribonucleoprotein Granule | Cytoplasmic Side | Cytoskeleton | Cytosol | Dendrite | Growth cone | Microtubule | Microtubule Associated Complex | Neurofibrillary Tangle | Neuronal Cell Body | Nuclear Periphery | Nuclear Speck | Nucleus | Peripheral membrane protein | Plasma Membrane | Tubulin Complex\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Fragment\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 10.133 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290885997,"sku":"SPR-445B","price":385.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016290918765,"sku":"SPR-445C","price":690.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016290951533,"sku":"SPR-445E","price":1435.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-445_Tau-Protein-Monomer-Protein-Thioflavin-T-assay-1.png?v=1770644818"},{"product_id":"alpha-synuclein-filaments-bhp11901150","title":"Alpha Synuclein Filaments","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e Alpha-synuclein (source species: Human; native localization: Cytoplasm | Membrane | Nucleus).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Alpha Synuclein Filaments\u003c\/p\u003e\u003cp\u003eAlpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlpha-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Membrane | Nucleus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e ~14.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016290984301,"sku":"SPR-450B","price":390.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016291017069,"sku":"SPR-450C","price":700.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016291049837,"sku":"SPR-450E","price":1455.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-450_Alpha-Synuclein-Protein-Filaments-Protein-TEM-2.png?v=1770644819"},{"product_id":"transthyretin-ttr-l55p-variant-monomers-bhp11901153","title":"Transthyretin (TTR) L55P Variant Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRANSTHYRETIN\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e TRANSTHYRETIN (source species: Human; native localization: Cytoplasm | Extracellular exosome | Extracellular Region | Lysosome).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Transthyretin (TTR) L55P Variant Monomers\u003c\/p\u003e\u003cp\u003eTransthyretin is a transport protein in the serum and cerebospinal fluid that carried the thyroid hormone Thyroxine and retinol-binding protein bound to retinol. TTR misfolding and aggregation is known to be associated with the amyloiddiseases SSA, FAP and FAC (1-5). TTR is also thought to have beneficial side effects, such as binding to beta-amyloid protein, preventing beta-amyloid from accumulating into the plaques associated with Alzheimer's Disease (6). The L55P variant TTR is distinct from the other variants in that the L55P tetramer can dissociate to the monomeric amyloidogenic intermediate and form fibril precursors (7).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRANSTHYRETIN\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Extracellular exosome | Extracellular Region | Lysosome\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 13.876 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016291082605,"sku":"SPR-451B","price":430.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016291115373,"sku":"SPR-451C","price":770.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016291148141,"sku":"SPR-451E","price":1605.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-451_Transthyretin-Protein-SDS-PAGE-1.png?v=1770640183"},{"product_id":"transthyretin-ttr-y78f-variant-monomers-bhp11901156","title":"Transthyretin (TTR) Y78F Variant Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRANSTHYRETIN\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e TRANSTHYRETIN (source species: Human; native localization: Cytoplasm | Extracellular exosome | Extracellular Region | Lysosome).\u003c\/p\u003e\u003cp\u003eHuman Recombinant Transthyretin (TTR) Y78F Variant Monomers\u003c\/p\u003e\u003cp\u003eTransthyretin is a transport protein in the serum and cerebospinal fluid that carried the thyroid hormone Thyroxine and retinol-binding protein bound to retinol. TTR misfolding and aggregation is known to be associated with the amyloiddiseases SSA, FAP and FAC (1-5). TTR is also thought to have beneficial side effects, such as binding to beta-amyloid protein, preventing beta-amyloid from accumulating into the plaques associated with Alzheimer's Disease (6).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRANSTHYRETIN\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm | Extracellular exosome | Extracellular Region | Lysosome\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 13.876 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. 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Beta synuclein is suggested to be an inhibitor of alpha synuclein aggregation- protecting the central nervous system from the neurotoxin effects of alpha synuclein (3).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBeta-synuclein\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (native):\u003c\/strong\u003e Cytoplasm\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e Full length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 14.28 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Ion-exchange Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e PBS pH 7.4\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. 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