Anti-Hsp90 Antibody (11113)
Anti-Hsp90 Antibody (11113)
Product No.: 11113
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Clone 4F3.E8 Target Hsp90α Formats AvailableView All Product Type Monoclonal Alternate Names EC 3.6.4.10, Heat shock 86 kDa, HSP 86, HSP86, Lipopolysaccharide-associated protein 2, LAP-2, LPS-associated protein 2, Renal carcinoma antigen NY-REN-38 Isotype Mouse IgG2a Applications ELISA , IHC , IP , WB |
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Antibody DetailsProduct DetailsReactive Species Human/Mouse/Rat Host Species Mouse Immunogen Recombinant human Hsp90 purified from E. coli. Product Concentration Lot Specific Formulation This monoclonal antibody is formulated in phosphate buffered saline (PBS) pH 7.2 - 7.4 with no carrier protein or preservatives added. State of Matter Liquid Product Preparation Antibodies are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates. Storage and Handling Upon initial thawing, appropriately aliquot and store at -80°C. For long-term storage, keep at -80°C. Avoid repeated freeze-thaw cycles. Country of Origin USA Shipping Next Day 2-8°C Applications and Recommended Usage? Quality Tested by Leinco Immunoblotting: use at 0.5-1ug/ml. A band of ~90 kDa is detected
User should determine optimal concentrations for their application. Positive control: Heat-shocked HeLa cell lysate. Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change. DescriptionDescriptionSpecificity This antibody recognizes human, mouse, and rat Hsp90α and β. Other species have not been tested. Background Hsp90 is an abundantly and ubiquitously expressed heat shock protein found in all eukaryotic cells. It exists in two principal forms, α and β, which share 85% sequence homology. Both forms are expressed in the cytosol. Hsp90α exists primarily as a homodimer while Hsp90β exists mainly as a monomer. Hsp90 plays a role in folding, assembly, maturation, and stabilization of specific proteins as a key component of a chaperone complex. Most of the Hsp90-regulated proteins that have been identified are involved in cell signaling; kinases, v-Src, Wee1, c-Raf, and p53 are some examples. When bound to ATP, Hsp90 interacts with co- chaperones Cdc37, p23, and various immunophilin-like proteins to form complexes that stabilize and protect target proteins from proteasomal degradation. Function 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 rPubMed:11274138, PubMed:11276205, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:20628368, PubMed:24613385, PubMed:25609812, PubMed:27353360, PubMed:29127155, PubMed:25973397, PubMed:26991466, PubMed:27295069}. NCBI Gene Bank ID UniProt.org Research Area Heat Shock & Stress Proteins References & CitationsTechnical ProtocolsCertificate of Analysis |
Formats Available
Products are for research use only. Not for use in diagnostic or therapeutic procedures.