{"product_id":"recombinant-human-heat-shock-cognate-71-kda-protein-hspa8-bhp10507846","title":"Recombinant Human Heat shock cognate 71 kDa protein (HSPA8)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eThis Recombinant Protein provides recombinant \u003cstrong\u003eHSPA8\u003c\/strong\u003e from Homo sapiens (Human), produced in Yeast (region 2-646aa). 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 2-646aa (domain boundaries can affect binding\/activity readouts).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression host:\u003c\/strong\u003e Yeast (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\u003eAlso reported as Heat shock 70 kDa protein 8 (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1) (HSC70) (HSP73) (HSPA10). Molecular 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 co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 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. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s, the nucleotide exchange factors such as BAG1\/2\/3, and the TPR domain chaperones such as HOPX and STUB1. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eActivity assay development for kinetics, substrate scope, and inhibitor\/activator profiling.\u003c\/li\u003e\n\u003cli\u003eUse of recombinant standards to improve assay calibration and cross-study comparability.\u003c\/li\u003e\n\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 co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 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. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s, the nucleotide exchange factors such as BAG1\/2\/3, and the TPR domain chaperones such as HOPX and STUB1. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1.\u003c\/p\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eStandard curve or spike-in reference for quantitative assays involving HSPA8\u003c\/li\u003e\n\u003cli\u003eEnzymatic activity measurements with defined substrates\/cofactors (assay-dependent)\u003c\/li\u003e\n\u003cli\u003eCompound screening using concentration–response concepts (assay-dependent)\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 P11142 — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P11142 - NCBI Gene search: HSPA8 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HSPA8 - Ensembl search: HSPA8 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HSPA8 - 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":53053426106733,"sku":"CSB-YP010829HU-1MG","price":2959.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53053572743533,"sku":"CSB-YP010829HU-100UG","price":694.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53053572776301,"sku":"CSB-YP010829HU-20UG","price":368.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-YP010829HU-SDS.jpg?v=1772177720","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-human-heat-shock-cognate-71-kda-protein-hspa8-bhp10507846","provider":"BioHippo","version":"1.0","type":"link"}