HSP90 alpha Antibody from ROCKLAND IMMUNOCHEMICALS INC.

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Antigenic SpecificityHSP90 alpha
CloneHyb-K41009
Host SpeciesMouse
Reactive Specieshuman, mouse, rat
IsotypeIgG2a
FormatProtein G purified
Size100 µg
Concentration1mg/mL
ApplicationsELISA, Immunohistochemistry, Western Blot
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DescriptionAnti-Hsp90α Antibody was purified by Protein G chromatography. A BLAST analysis was used to suggest cross-reactivity with Hsp90 from Human (alpha-specific) sources based on 100% homology with the immunizing sequence. Cross-reactivity with Hsp90 from other sources has not been determined. Heat Shock research. 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. 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. 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.
ImmunogenHsp90 α Antibody was produced in mice by repeated immunizations raised against recombinant human Hsp90alpha.
Other Namesmouse anti-Anti-Hsp90 alpha, mouse anti-Anti-Hsp90a, mouse anti-heat shock protein 90 alpha, Hsp86, Hsp89A, Hsp90AA1, Hsp90Alpha, HspC1, HSPCA, HspCAL3, Heat shock protein HSP 90-alpha, Heat shock 86 kDa, HSP 86, HSP86, Renal carcinoma antigen NY-REN-38, HSP90AA1, HSP90A, HSPC1, HSPCA
Gene, Accession #HSP90AA1, Gene ID: 3320, NCBI: NP_001017963.2, UniProt: P07900
Catalog #209-301-F70
Price$485
Order / More InfoHSP90 alpha Antibody from ROCKLAND IMMUNOCHEMICALS INC.
Product Specific Referencesn/a
ROCKLAND IMMUNOCHEMICALS INC.
ROCKLAND IMMUNOCHEMICALS INC.
ROCKLAND IMMUNOCHEMICALS INC.
PO Box 5199
Limerick PA 19468
P: 484-791-3823
P: 800.656.7625
F: 484.369.8654

orders@rockland.com
Technical Support: tech@rockland.com

https://www.rockland.com/

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