HSP90 Antibody (D7A)

Product Discontinued

HSP90 Antibody (D7A) Summary

• Immunogen: Full length protein HSP90 purified from chicken brain
• Localization: Cytoplasm , Melanosome
• Specificity: Can isolate complexes of HSP90, Src kinase and cec37.
• Isotype: IgG1
• Clonality: Monoclonal
• Host: Mouse
• Gene: HSP90AA1
• Purity: Protein G purified

Applications/Dilutions

• Dilutions:
  • ELISA
  • Immunohistochemistry
  • Immunohistochemistry-Paraffin
  • Immunoprecipitation 5ug
  • Microarray
  • Western Blot 1:500
• Application Notes: 2 ug/ml was sufficient for detection of HSP90alpha in 20 ug of heat shocked HeLa cell lysate as well as in 100 ng of human HSP90alpha protein by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.
• Theoretical MW: 90 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: PBS pH 7.2, 50% glycerol
• Preservative: 0.09% Sodium Azide
• Concentration: 1 mg/ml
• Purity: Protein G purified

Alternate Names for HSP90 Antibody (D7A)

• FLJ31884
• Heat shock 86 kDa
• heat shock 90kD protein 1, alpha
• heat shock 90kD protein 1, alpha-like 4
• heat shock 90kD protein, alpha-like 4
• heat shock 90kDa protein 1, alpha
• heat shock protein 90kDa alpha (cytosolic), class A member 1
• heat shock protein HSP 90-alpha
• Hsp89
• HSP90
• HSP90AHSP86
• HSP90N
• HSPC1HSP 86
• HSPCAHSP89A
• HSPCAL1
• HSPCAL4
• HSPN
• LAP2
• Renal carcinoma antigen NY-REN-38

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).

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Bioinformatics

• Gene Symbol: HSP90AA1