{"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}],"url":"https:\/\/www.ebiohippo.com\/products\/hsp90-protein-bhp11900043","provider":"BioHippo","version":"1.0","type":"link"}