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Anti-HSP90AA1 Antibody D7A
Also for HSP90AA1 (NM_001017963)
|Full length protein Hsp90 purified from chicken brain|
|Bovine, Chicken, Human, Mouse, Porcine (Pig), Rat, Rabbit
||WB: 1:500, IP: 5ug with 20ul Protein A beads
|PBS, 50% glycerol, 0.09% sodium azide |
|Protein G Purified
|Recognizes 90kDa proteins corresponding to the molecular mass of Hsp90. Hsp90a specific for human samples. Can isolate complexes of Hsp90, Src kinase and cec37.
|Homo sapiens heat shock protein 90kDa alpha (cytosolic), class A member 1 (HSP90AA1), transcript variant 1|
|EL52; HSP86; Hsp89; HSP89A; Hsp90; HSP90A; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; LAP-2; LAP2|
|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 known 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. 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 immune-oadsorption 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 .|
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Western blot analysis of Hsp90 in rat tissue lysates using a 1:1000 dilution of the antibody
IHC staining of inflammatory cells in mouse colon tissue.