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Antigenic Specificity | HSP90 complex |
Clone | 8D3 |
Host Species | Mouse |
Reactive Species | human, mouse, rat, rabbit |
Isotype | IgM |
Format | PEG purified |
Size | 200 µg |
Concentration | 1mg/mL |
Applications | IF, IP |
Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
Description | Anti-Hsp90 complex Antibody was PEG Purified. A BLAST analysis was used to suggest cross-reactivity with Hsp90 from Human, Mouse, Rat, and Rabbit sources based on 100% homology with the immunizing sequence. Cross-reactivity with Hsp90 complex from other sources has not been determined. Heat Shock research. 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 (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. |
Immunogen | Hsp90 complex Antibody was produced in mice by repeated immunizations raised against the ah receptor (Aryl hydrocarbon receptor). |
Other Names | Hsp84, Hsp90, Hsp90 beta, Hsp90B, HspC2, HSPCB, Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, HSP90AB1, HSP90B, HSPC2, HSPCB |
Gene, Accession # | HSP90AA1, Gene ID: 3320, NCBI: NP_001017963.2, UniProt: P07900 |
Catalog # | 200-301-F73 |
Price | $619 |
Order / More Info | HSP90 complex Antibody from ROCKLAND IMMUNOCHEMICALS INC. |
Product Specific References | n/a |