HSP90 beta Antibody from ROCKLAND IMMUNOCHEMICALS INC.

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Antigenic SpecificityHSP90 beta
CloneHyb-K3701
Host SpeciesMouse
Reactive Specieshuman, mouse
IsotypeIgM
FormatProtein G purified
Size100 µg
Concentration1.0 mg/mL
ApplicationsELISA, Immunohistochemistry, Western Blot
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DescriptionAnti-Hsp90β Antibody was purified by Protein G chromatography. A BLAST analysis was used to suggest cross-reactivity with Hsp90β from Human (beta specific) based on 100% homology with the immunizing sequence. Cross-reactivity with Hsp90β from other sources has not been determined. Heat Shock research. HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment. Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. 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. 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. 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 beta Antibody was produced in mice by repeated immunizations raised against recombinant human Hsp90beta.
Other Namesmouse anti-Anti-Hsp90 beta, mouse anti-Anti-Hsp90b, mouse anti-heat shock protein 90 beta, Hsp84, Hsp90, Hsp90 beta, Hsp90B, HspC2, HSPCB, Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, HSP90AB1, HSP90B, HSPC2, HSPCB, HSP90β
Gene, Accession #HSP90AB1, Gene ID: 3326, NCBI: NP_031381.2, UniProt: P08238
Catalog #209-301-F71
Price$485
Order / More InfoHSP90 beta 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

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