{"product_id":"hsp90-recombinant-rabbit-mab-s-5412-s0b60242","title":"HSP90 Recombinant Rabbit mAb (S-5412)","description":"\u003ch4\u003eProduct Specification\u003c\/h4\u003e\u003cdiv class=\"responsive-table product-detail-table details-table\"\u003e\n\u003cbr\u003e\u003ctable style=\"width: 100%; height: auto;\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eHost\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eRabbit\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eAntigen\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eHSP90\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eHeat shock protein HSP 90-alpha; Heat shock 86 kDa (HSP 86; HSP86); Heat shock protein family C member 1; Lipopolysaccharide-associated protein 2 (LAP-2; LPS-associated protein 2); Renal carcinoma antigen NY-REN-38; HSP90A; HSPC1; HSPCA; HSP90AA1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eLocation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eCytoplasm, Nucleus, Cell membrane\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eP07900\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eClone Number\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eS-5412\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eAntibody Type\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eRecombinant mAb\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eIsotype\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eIgG\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eApplication\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eWB, IHC-P\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eReactivity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eHu, Ms, Rt\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003ePositive Sample\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eHeLa, HEK-293, MCF7, Jurkat, LnCaP, HepG2, NIH\/3T3, RAW264.7, mouse brain, C6, PC-12, rat brain\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003ePurification\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eProtein A\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eConcentration\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e0.5 mg\/ml\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eConjugation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eUnconjugated\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003ePhysical Appearance\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eLiquid\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eStorage Buffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e\u003cp\u003ePBS, 40% Glycerol, 0.05% BSA, 0.02% sodium azide\u003c\/p\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eStability \u0026amp; Storage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e\u003cp\u003e12 months from date of receipt \/ reconstitution, -20 °C as supplied\u003c\/p\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e\n\u003c\/div\u003e\u003ch4\u003eDilution\u003c\/h4\u003e\u003cdiv class=\"responsive-table product-detail-table details-table\"\u003e\n\u003cbr\u003e\u003ctable style=\"width: 60%; height: auto;\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd\u003e\u003cstrong\u003eapplication\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd\u003e\u003cstrong\u003edilution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd\u003e\u003cstrong\u003especies\u003c\/strong\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003eWB\u003c\/td\u003e\n\u003ctd\u003e1:5000-1:50000\u003c\/td\u003e\n\u003ctd\u003eHu, Ms, Rt\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003eIHC-P\u003c\/td\u003e\n\u003ctd\u003e1: 2000\u003c\/td\u003e\n\u003ctd\u003eHu, Ms, Rt\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e\n\u003c\/div\u003e\u003ch4\u003eBackground\u003c\/h4\u003e\u003cdiv\u003e\u003cp\u003e\u003cspan\u003eHSP90 (Heat Shock Protein 90) is one of the most abundant and functionally critical molecular chaperones in eukaryotic cells, belonging to the HSP90 family (which in mammals mainly comprises cytosolic HSP90α and HSP90β, endoplasmic reticulum-resident GRP94, and mitochondrial TRAP1). Its core function is to act as a \"conformational switch\" that, through ATP-dependent conformational changes, assists its \"client proteins\"—numbering in the hundreds, the vast majority of which are involved in signal transduction (such as kinases, steroid hormone receptors, and transcription factors)—in proper folding, maturation, and maintenance of active conformations, while also preventing these client proteins from being degraded due to misfolding. HSP90 does not work in isolation; it collaborates with multiple co-chaperones (such as HSP70, HSP40) and immunophilins to form dynamic multi-subunit complexes, orchestrating a precise \"folding cycle\" in which it alternates between open and closed conformations driven by ATP hydrolysis, thereby capturing, loading, and releasing substrate proteins. This process is particularly crucial under cellular stress conditions (such as heat shock, oxidative stress, or heavy metal exposure), when HSP90 expression is upregulated to protect the proteome from damage, while it also participates in important physiological and pathological processes including cell cycle regulation, cell survival, and tumorigenesis. Precisely because of its central role in maintaining the stability of multiple oncogenic proteins, HSP90 has become an important target in cancer therapy; various natural-product-derived inhibitors (such as geldanamycin derivatives, radicicol, and resorcinol compounds) have been developed and entered clinical studies, aiming to simultaneously degrade multiple oncogenic client proteins by blocking its ATPase activity, demonstrating broad-spectrum antitumor potential—however, their clinical application remains challenged by side effects including hepatotoxicity, ocular toxicity, and heat shock response rebound.\u003c\/span\u003e\u003c\/p\u003e\u003c\/div\u003e","brand":"Starter","offers":[{"title":"25μl","offer_id":42934767550539,"sku":"S0B60242-25μl","price":70.0,"currency_code":"USD","in_stock":true},{"title":"100μl","offer_id":42934767583307,"sku":"S0B60242-100μl","price":150.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0590\/8375\/1499\/files\/AntBioImage_2e0bf484-fc1d-45f6-ab20-46422baebc91.png?v=1784786417","url":"https:\/\/www.antbioinc.com\/products\/hsp90-recombinant-rabbit-mab-s-5412-s0b60242","provider":"AntBio","version":"1.0","type":"link"}