Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

protein

HSP90β (human), (recombinant)

ADI-SPP-777-D

50 µg

ADI-SPP-777-D

HSP90β (human), (recombinant)

Protein

50 µg

25677667

The 90 kDa molecular chaperone family includes 90 kDa heat shock protein HSP90 and 94 kDa glucose-regulated protein Grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells express inducible HSP90a and constitutive HSP90β isoforms that are encoded by separate genes. The amino acid sequences of human and yeast HSP90a are 85% and 90% homologous to those of HSP90β, respectively. All known members of the HSP90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. HSP90 functions as part of the cell’s powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, HSP90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control by serving as a chaperone for many key signaling molecules including steroid receptors, cell cycle kinases involved in signal transduction, and p53. As many of these client proteins are known oncogenes, Hsp90 inhibitors such as 17-AAG, a geldanamycin analog, have been of benefit in the treatment of many cancers.

HSP84, Heat shock protein 90β

≥85% (SDS-PAGE; Western blot)

Liquid. In 20mM TRIS, pH 7.5, containing 500mM sodium chloride, 5% glycerol, and 1mM DTT.

Western blot control.

WB

-80°C