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SRP0183 Sigma

Hsp90b Active human

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

Synonym: HSP84, HSP90Beta, HSPC2, Heat shock protein 90 kDa β



Related Categories Cell Biology, Cell Signaling and Neuroscience, Cell Stress, Chaperonins and Heat Shock Proteins, Heat Shock and Related Proteins,
recombinant   expressed in E. coli
assay   ≥80% (SDS-PAGE)
form   aqueous solution
mol wt   mol wt 83 kDa
NCBI accession no.   AY359878
shipped in   dry ice
storage temp.   −70°C
Gene Information   human ... HSP90AB1(3326)



Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Preparation Note

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

Physical form

Formulated in 25 mM Tris-HCl, pH 7.5, 100mM NaCl, 0.05% Tween 20, 20% glycerol and 3 mM DTT.

Biochem/physiol Actions

Hsp90 (heat shock protein 90) is needed for folding, maturation, transport, and degradation of various proteins, particularly signaling molecules, steroid receptors, and transcription factors. Hsp90b (Hsp90 β) is secreted by various cells and works as a chaperone for selected surface-associated or secreted proteins. It acts as a chaperone for matrix metalloproteinases and extracellular matrix proteins, and helps in cell motility. Suppression of the Hsp90b activity is suggested as a therapeutic approach for various cancers and inflammatory diseases.

General description

Hsp90b (heat shock protein 90-β) is a constitutive cytosolic isoform of Hsp90. The gene is mapped to human chromosome 6p21.1. Hsp90b is an ATP-dependent molecular chaperone and is upregulated in many tumor cells.
Human Heat Shock Protein 90β (GenBank Accession No. AY359878), full length with C-terminal His tag, MW = 83kDa, expressed in an Escherichia coli expression system.

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Safety Information

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Certificate of Analysis

Protocols & Articles
Peer-Reviewed Papers


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