Labprice Monoclonal antibody for HSP90 alpha/beta

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 (1). Despite the similarities, HSP90? exists predominantly as a homodimer while HSP90? 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 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 (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.

Description: A monoclonal antibody from clone Hyb-K41220A against Human HSP90 alpha/beta. The host species for the production of this antibody is Mouse. The antigen used for immunization is Human Recombinant human HSP90alpha; Specificity mapped to amino acids 291-304. The antibody is tested and validated for WB, IHC, ICC/IF, ELISA assays with the following recommended dilutions: WB (1:1000), IHC (1:100), ICC/IF (1:100). This MAb for HSP90 alpha/beta is conjugated with Dylight 350.

Shipped on ice packs at +4ºC . Upon receiving the antibody store it at -20ºC.
The gross weight of the package is 1.4 kg. and the net weight of the product is 0.1 grams.
The item is not hazardous according to both ADR and UN. Its tariff code is 3002.15.0000 (Immunological products, put up in measured doses or in forms or packings for retail sale). The UNSPSC code of the product is 12352203 (Antibodies).

This product is not for human or animal treatment or consumption. Not for use in diagnostics or therapeutics. For in vitro research use only.