{"product_id":"recombinant-mouse-heat-shock-cognate-71-kda-protein-hspa8-bhp10510272","title":"Recombinant Mouse Heat shock cognate 71 kDa protein (Hspa8)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003eRecombinant Mouse Heat shock cognate 71 kDa protein (Hspa8) is a recombinant protein reagent derived from Mus musculus (Mouse) and produced in E.coli. It is commonly used to support Signal Transduction research by enabling binding assays, assay development and protein–protein interaction studies in controlled in vitro settings.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 2-646aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression host can influence folding and the presence\/absence of post-translational modifications.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eTag \/ fusion:\u003c\/strong\u003e N-terminal 10xHis-tagged and C-terminal Myc-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular weight (reported):\u003c\/strong\u003e 78.2 kDa. Apparent size may vary with tags, processing, and gel conditions.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eWhen comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.\u003c\/p\u003e \u003ch2\u003eBiological background\u003c\/h2\u003e \u003cp\u003eThe gene commonly associated with this target is \u003cstrong\u003eHspa8\u003c\/strong\u003e. Hspa8 refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Mus musculus (Mouse) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt\/NCBI) and the recent literature for the specific organism and isoform.\u003c\/p\u003e \u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e \u003cli\u003eUsing recombinant proteins to enable quantitative binding measurements and reagent benchmarking.\u003c\/li\u003e \u003cli\u003eStudying domain- and isoform-specific effects in pathway models and interaction networks.\u003c\/li\u003e \u003cli\u003eDeveloping robust, reproducible assays that connect molecular readouts to cellular phenotypes.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003e\u003cstrong\u003eRelevance:\u003c\/strong\u003e 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 (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1\/2\/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. 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 (LPS) 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. Interacts with VGF-derived peptide TLQP-21.\u003c\/p\u003e \u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e \u003cli\u003eAssay and standard development for immunoassays or binding-based detection methods.\u003c\/li\u003e \u003cli\u003eProtein–protein interaction studies (e.g., receptor–ligand or complex assembly) using purified components.\u003c\/li\u003e \u003cli\u003eStructure–function analysis, including domain mapping or evaluation of sequence variants.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eIn quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative\/positive controls and, where possible, orthogonal assay formats that support the same conclusion.\u003c\/p\u003e \u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e \u003cli\u003eRecombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.\u003c\/li\u003e \u003cli\u003eTag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.\u003c\/li\u003e \u003cli\u003eSpecies and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.\u003c\/li\u003e \u003cli\u003eE. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.\u003c\/li\u003e \u003c\/ul\u003e \u003c!-- Sources (internal): - UniProtKB entry for P63017 — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P63017\/entry - NCBI Gene search (Hspa8) — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=Hspa8 - PubMed search (Hspa8) — NCBI — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=Hspa8 - RCSB PDB search (Hspa8) — RCSB PDB — https:\/\/www.rcsb.org\/search?query=Hspa8 - Reactome Pathway Browser — Reactome — https:\/\/reactome.org\/ --\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53065315352941,"sku":"CSB-EP010829MO-1MG","price":2466.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53065482568045,"sku":"CSB-EP010829MO-100UG","price":729.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53065482600813,"sku":"CSB-EP010829MO-20UG","price":388.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-EP010829MO-SDS.jpg?v=1772476562","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-mouse-heat-shock-cognate-71-kda-protein-hspa8-bhp10510272","provider":"BioHippo","version":"1.0","type":"link"}