{"product_id":"recombinant-danio-rerio-heat-shock-protein-hsp-90-alpha-1-hsp90a-1-partial-bhp10507046","title":"Recombinant Danio rerio Heat shock protein HSP 90-alpha 1 (hsp90a.1), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eThis Recombinant Protein provides recombinant \u003cstrong\u003ehsp90a.1\u003c\/strong\u003e from Danio rerio (Zebrafish) (Brachydanio rerio), produced in Baculovirus (region 151-355aa). 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 151-355aa (domain boundaries can affect binding\/activity readouts).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression host:\u003c\/strong\u003e Baculovirus (may differ from native PTMs\/processing).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag(s):\u003c\/strong\u003e His, Myc (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 hsp90 (hsp90a) (hsp90aa1). 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 that is linked to its ATPase activity which is essential for its chaperone 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. Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.\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 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 that is linked to its ATPase activity which is essential for its chaperone 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. Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.\u003c\/p\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eStandard curve or spike-in reference for quantitative assays involving hsp90a.1\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 Q90474 — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q90474 - NCBI Gene search: hsp90a.1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=hsp90a.1 - Ensembl search: hsp90a.1 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=hsp90a.1 - 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":53053401694573,"sku":"CSB-BP838557DIL-1MG","price":3278.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53053523231085,"sku":"CSB-BP838557DIL-100UG","price":1478.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53053523263853,"sku":"CSB-BP838557DIL-20UG","price":528.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-BP838557DIL-SDS.jpg?v=1772177629","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-danio-rerio-heat-shock-protein-hsp-90-alpha-1-hsp90a-1-partial-bhp10507046","provider":"BioHippo","version":"1.0","type":"link"}