HSP90α, His-tag

Catalog #: 50290
Size: 200 µg
$385
Species: Human
Host Species: E. coli
MW: 85.5 kDa
Genbank #: NM_005348
Tag(s): C-terminal His-tag
a.a: full length
Background:
Hsp90 (90 kDa heat shock protein) is a molecular chaperone that aids protein folding and quality control for a large number of client proteins. Functional Hsp90 operates as dimer and has intrinsic ATPase activity. The Hsp90 dimer acts in concert with other chaperones (e.g. Hsp70) and is regulated by a number of co-chaperones/accessory proteins (e.g. Hop, cdc37). Hsp90 has been shown to interact with > 100 proteins and some notable clients include kinases (e.g. Raf-1), nuclear hormone receptors (e.g. estrogen receptors), transcription factors (e.g. p53), GPCRs (e.g. CB2 receptors) and ion channels (e.g. CFTR). In humans, the Hsp90beta isoform is constitutively expressed whereas the Hsp90alpha isoforms is expressed under stress conditions. Hsp90 plays an important role in some tumor cell types by stabilising mutated oncogenic proteins.
Description:
Human Heat Shock Protein 90α (GenBank Accession No. NM_005348), full length with C-terminal His-tag, MW = 85.5 kDa, expressed in an E. coli expression system.
UniProt
P07900
Synonym(s):
HSP90a, Heat Shock Protein 90a, HSP90alpha, HSP90α
Specific Activity:
Kd = 11.8 nM.
Assay Conditions:

Assayed using the BPS Hsp90α Assay kit, Cat. # 50293. A 95 µl reaction mix (20 mM HEPES pH 7.3, 50 mM KCl, 5 mM MgCl2, 20 mM Na2MoO4, 0.01% Triton X-100, 100 µg/ml bovine serum albumin, 2 mM DTT, 0-30 nM Hsp90α) + 5 µl FITC-geldanamycin was incubated for 4 hrs at 4°C. Fluorescent polarization was measured at room temperature (λexc=485 nm, λem=528 nm).

Formulation:
45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 225 mM imidazole, 10% glycerol and 3 mM DTT
Format:
Aqueous buffer solution
Storage / Stability:
At least 6 months at –80°C.
Application(s):
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Reference(s):

1. Wayne N. and Bolon D.N. J Biol Chem. 2007 Nov 30;282(48):35386-95.
2. Pearl L.H., et al. Biochem J. 2008 Mar 15;410(3):439-53.

Application Reference(s):
1. The quinone methide aurin is a heat shock response inducer that causes proteotoxic stress and Noxa-dependent apoptosis in malignant melanoma cells (2015)
2. Herbimycins D-F, ansamycin analogues from Streptomyces sp. RM-7-15 (2013)

Warning(s):
Avoid freeze/thaw cycles
Scientific Category:
Heat Shock Proteins
Product Type:
Recombinant Protein
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