{"product_id":"recombinant-chicken-heat-shock-70-kda-protein-partial-bhp10508202","title":"Recombinant Chicken Heat shock 70 kDa protein, partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eThis Recombinant Protein provides recombinant \u003cstrong\u003eHSP70\u003c\/strong\u003e from Gallus gallus (Chicken), produced in E.coli (region 3-389aa). It is commonly used as a defined reagent for assay development, binding studies, and mechanistic research (RUO).\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRegion:\u003c\/strong\u003e 3-389aa (domain boundaries can affect binding\/activity readouts).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression host:\u003c\/strong\u003e E.coli (may differ from native PTMs\/processing).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag(s):\u003c\/strong\u003e His (supports purification\/detection; consider tag effects in controls).\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003eMolecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\u003cli\u003eUse of recombinant standards to improve assay calibration and cross-study comparability.\u003c\/li\u003e\u003c\/ul\u003e\u003cp\u003eMolecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.\u003c\/p\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eStandard curve or spike-in reference for quantitative assays involving HSP70\u003c\/li\u003e\n\u003cli\u003eBinding and specificity benchmarking for detection reagents (conceptual)\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eRecombinant constructs may not capture all native isoforms or PTMs.\u003c\/li\u003e\n\u003cli\u003eConsider tag- or host-related effects when interpreting binding or activity.\u003c\/li\u003e\n\u003cli\u003eUse appropriate blanks and matrix\/control concepts to separate signal from background.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - UniProtKB P08106 — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P08106 - NCBI Gene search: HSP70 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HSP70 - Ensembl search: HSP70 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HSP70 - Reactome Pathway Browser — Reactome — https:\/\/reactome.org\/ - NCBI Bookshelf — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/books\/ --\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53053436756333,"sku":"CSB-EP362326CH-1MG","price":2466.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53053595222381,"sku":"CSB-EP362326CH-100UG","price":729.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53053595255149,"sku":"CSB-EP362326CH-20UG","price":388.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-EP362326CH-SDS.jpg?v=1772177755","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-chicken-heat-shock-70-kda-protein-partial-bhp10508202","provider":"BioHippo","version":"1.0","type":"link"}