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Anti-HSP90AA1 Antibody 2G5.G3
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Also for HSP90AA1 (NM_001017963)
|Human, Mouse, Rat. Other species not tested yet.
|PBS pH7.2, 50% glycerol|
|Protein G Purified
|Hsp90a-specific (>96% a-specific by ELISA)
|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|
Entrez Gene 3320 Human
Entrez Gene 15519 Mouse
Entrez Gene 299331 Rat
|HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms and , which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment . Despite the similarities, HSP90 exists predominantly as a homodimer while HSP90 exists mainly as a monomer. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% 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 .|
|Druggable Genome Antigen processing and presentationNOD-like receptor signaling pathwayProgesterone-mediated oocyte maturationPathways in cancerProstate cancer|
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Western blot analysis of Hsp90Alpha in rat tissues, using a 1:1000 dilution of the antibody
Hsp90Alpha visulaized using the antibody