{"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","url":"https:\/\/www.ebiohippo.com\/products\/hsp70-protein-bhp11900031","provider":"BioHippo","version":"1.0","type":"link"}