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Anti-HSP90AB1 Antibody 8D3
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Also for HSP90AB1 (NM_007355)
|Ah receptor (Aryl hydrocarbon receptor)|
|Human, Mouse, Rat, Rabbit. Not tested on other species.
|PBS, 50% glycerol, 0.09% sodium azide |
|Immunoprecipitates 90kDa proteins corresponding to the molecular mass of Hsp90. Co-immunoprecipitates Hsp90 complexes, including Hsp70, Hop, Ah receptors, glucocorticoid receptors, heme-regulated eukaryotic initiation factor 2a (eIF-2a) kinase (HRI).
|Homo sapiens heat shock protein 90kDa alpha (cytosolic), class B member 1 (HSP90AB1), transcript variant 2|
|D6S182; HSP84; HSP90B; HSPC2; HSPCB|
Entrez Gene 3326 Human
Entrez Gene 15516 Mouse
Entrez Gene 301252 Rat
|Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex . Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (12% of cytosolic protein). It carries out a number of housekeeping functions including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90- regulated proteins that have been discovered to date are involved in cell signaling . The number of proteins now know to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5 When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function .|
|Stem cell - PluripotencyDruggable Genome Antigen processing and presentationNOD-like receptor signaling pathwayProgesterone-mediated oocyte maturationPathways in cancerProstate cancer|
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Hsp90 complex isolation (IP) from rabbit reticulocyte lysate (8D3), SDS PAGE.