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Antibodies

HSP90 Antibody, Clone H9010

Product Sizes
12 ug
SMC-107-12UG
200 ug
SMC-107-200UG
About this Product
SKU:
SMC-107
Additional Names:
HSP84 Antibody, HSP90 Antibody, HSP90 beta Antibody, HSP90B Antibody, HSPC2 Antibody, HSPCB Antibody
Application:
Antibody Microarray, ELISA, Immunocytochemistry, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blot
Buffer:
PBS
CE/IVD:
RUO
translate.label.attr.clone:
H9010
Clonality:
Monoclonal
Concentration:
1 mg/ml
Extra Details:
HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms A Alpha and B Beta, which share 85% sequence amino acid homology. The two isoforms of HSP90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90A Alpha exists predominantly as a homodimer while HSP90B Beta exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). 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 it's 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 (7-8). 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 (9). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Host:
Mouse
Immunogen:
Recombinant human HSP90beta
Isotype:
IgG2a
Purification:
Protein G Purified
Reactivities:
Avian, Canine, Fish, Hamster, Human, Mouse, Rabbit, Rat
Shipping Conditions:
Blue Ice
Specificity:
Detects 90kDa. Detects HSP90 beta in all reactive species except in Chicken, where it detects both alpha and beta isoforms.
Storage Conditions:
-20[o]C
Supplier:
StressMarq Biosciences
Type:
Antibody: Monoclonal Antibody