{"product_id":"recombinant-human-heat-shock-protein-hsp-90-beta-hsp90ab1-bhp10512813","title":"Recombinant Human Heat shock protein HSP 90-beta (HSP90AB1)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eRecombinant Human Heat shock protein HSP 90-beta (HSP90AB1) is a recombinant protein preparation from Homo sapiens (Human) designed for use in assay development, binding studies, and functional characterization. Key attributes such as expression system, expressed region, and affinity tag(s) help researchers match the reagent to specific experimental readouts.\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Baculovirus expression is commonly used for rapid, scalable production. For targets that require glycosylation or other post-translational modifications, consider how a prokaryotic system may affect folding or activity.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e The expressed fragment (2-724aa) focuses the reagent on a defined domain\/segment, which can influence binding interfaces and epitope availability.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag(s)\/format:\u003c\/strong\u003e His tags can support purification and detection in pull-down or binding assays; confirm that the tag position does not interfere with the interaction of interest.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e ≥85% (SDS-PAGE) provides a quick checkpoint for reagent quality in downstream analytical workflows.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Supplied as Liquid or Lyophilized powder; select the format that best fits your lab’s handling and aliquoting preferences.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eRecombinant design choices (expression host, fragment boundaries, and tag configuration) help balance yield, solubility, and assay compatibility. Choose conditions and controls that match the recombinant format to your experimental question.\u003c\/p\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSP90AB1\u003c\/strong\u003e has been reported to be involved in Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone involved in the phosphorylation\/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1\/IL-1; the translocation process is mediated by the cargo receptor TMED10. ; (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes. Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable).. When interpreting results, consider species context, domain architecture, and whether the recombinant format represents full-length or a defined region.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eAntigen and virulence-factor studies that compare strain- or domain-specific binding and immune recognition.\u003c\/li\u003e\n\u003cli\u003eUse of recombinant proteins as standards for quantitative assays and serology-oriented method development.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eBinding and interaction assays:\u003c\/strong\u003e quantify partner binding and rank conditions using plate-based formats or biophysical methods (SPR\/BLI).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEnzymology:\u003c\/strong\u003e assess catalytic activity and compare substrate preferences or inhibitor effects using appropriate controls.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAssay development:\u003c\/strong\u003e use as a standard, spike-in control, or positive control where consistent specifications are required.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eInterpretation typically relies on relative comparisons (treated vs control, mutant vs wild-type, or dose\/time series) using consistent sample handling and appropriate normalization.\u003c\/p\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePost-translational modifications:\u003c\/strong\u003e expression system can affect glycosylation and processing; interpret differences cautiously when comparing to native protein.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eIsoforms and domains:\u003c\/strong\u003e expressed regions may not capture all isoform-specific features; match fragment boundaries to your assay’s binding site.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eControls:\u003c\/strong\u003e include blank matrix controls, tag-only controls (where relevant), and orthogonal readouts (e.g., WB\/qPCR\/ELISA) to support interpretation.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - UniProt Knowledgebase entry for HSP90AB1 — UniProt — https:\/\/www.uniprot.org\/ - NCBI Gene for HSP90AB1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/ - RCSB Protein Data Bank — RCSB PDB — https:\/\/www.rcsb.org\/ - PubMed (reviews and primary literature) — NCBI — https:\/\/pubmed.ncbi.nlm.nih.gov\/ - Ensembl gene summary — Ensembl — https:\/\/www.ensembl.org\/ --\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53059029696877,"sku":"CSB-BP010808HU-1MG","price":3278.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53059161457005,"sku":"CSB-BP010808HU-100UG","price":1478.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53059161489773,"sku":"CSB-BP010808HU-20UG","price":528.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-BP010808HU-SDS.jpg?v=1772271386","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-human-heat-shock-protein-hsp-90-beta-hsp90ab1-bhp10512813","provider":"BioHippo","version":"1.0","type":"link"}