{"product_id":"cst-5087s","title":"CST,  5087S, HSP90 beta Antibody","description":"Polyclonal Antibody for studying HSP90B. Validated for Western Blotting. Highly specific and rigorously validated in-house, HSP90 beta Antibody (CST #5087) is ready to ship.\n\n\u003cb\u003eProduct Usage Information\u003c\/b\u003e\nWestern Blotting: 1:1000\n\u003cb\u003eStorage\u003c\/b\u003e\nSupplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg\/ml BSA and 50% glycerol. Store at -20°C. Do not aliquot the antibody.\n\u003cb\u003eProtocol\u003c\/b\u003e\nAvailable protocols: Western Blotting\n\u003cb\u003eSpecificity \/ Sensitivity\u003c\/b\u003e\nHSP90 beta Antibody detects endogenous levels of total HSP90β protein. This antibody does not cross-react with HSP90α.\nSpecies Reactivity: Human, Mouse, Rat, Monkey, Bovine\n\u003cb\u003eSource \/ Purification\u003c\/b\u003e\nPolyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the region surrounding Val473 of human HSP90β protein. Antibodies are purified by protein A and peptide affinity chromatography.\n\u003cb\u003eBackground\u003c\/b\u003e\nHSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70\/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70\/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).\n\u003cb\u003eAlternate Names\u003c\/b\u003e\nD6S182; FLJ26984; Heat shock 84 kDa; heat shock 90kD protein 1, beta; heat shock 90kDa protein 1, beta; heat shock protein 90 alpha family class B member 1; heat shock protein 90 kDa; heat shock protein 90kDa alpha (cytosolic), class B member 1; heat shock protein 90kDa alpha family class B member 1; heat shock protein beta; Heat shock protein HSP 90-beta; HS90B; HSP 84; HSP 90; HSP84; HSP90-BETA; HSP90AB1; HSP90B; HSPC2; HSPCB\n\n\u003cb\u003eSpecification\u003c\/b\u003e\n\nREACTIVITY: H M R Mk B\nSENSITIVITY: Endogenous\nMW (kDa): 90\nSOURCE: Rabbit","brand":"CST","offers":[{"title":"Default Title","offer_id":46799780806825,"sku":"5087S","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/products\/cst-5087s","provider":"Iright","version":"1.0","type":"link"}