Mouse Hsp90 Monoclonal Antibody | anti-HSP90AA1 antibody
Hsp90 Antibody: ATTO 390
Immunohistochemistry (IHC)
(Immunohistochemistry analysis using Mouse Anti-Hsp90 Monoclonal Antibody, Clone D7alpha. Tissue: colon carcinoma. Species: Human. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp90 Monoclonal Antibody at 1:100000 for 12 hours at 4 degree C. Secondary Antibody: Biotin Goat Anti-Mouse at 1:2000 for 1 hour at RT. Counterstain: Mayer Hematoxylin (purple/blue) nuclear stain at 200 ul for 2 minutes at RT. Magnification: 40x.)
Immunohistochemistry (IHC)
(Immunohistochemistry analysis using Mouse Anti-Hsp90 Monoclonal Antibody, Clone D7alpha. Tissue: inflamed colon. Species: Mouse. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp90 Monoclonal Antibody at 1:100000 for 12 hours at 4 degree C. Secondary Antibody: Biotin Goat Anti-Mouse at 1:2000 for 1 hour at RT. Counterstain: Mayer Hematoxylin (purple/blue) nuclear stain at 200 ul for 2 minutes at RT. Localization: Inflammatory cells. Magnification: 40x. Inflammatory cells.)
Western Blot (WB)
(Western Blot analysis of Rat cell lysates showing detection of Hsp90 protein using Mouse Anti-Hsp90 Monoclonal Antibody, Clone D7Alpha. Load: 15 ug. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp90 Monoclonal Antibody at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.)
Scientific Background: 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 (4-7). 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 (8-9). 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(6). 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-adsorption 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 (10).
NCBI and Uniprot Product Information
Uniprot Description
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.
