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Encompassing Amino Acids: full length
Applications: Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Assay Conditions: Buffer contains 0.1M HEPES, pH 7.4, 0.25M MgCl2, 0.25M KCl, 0.1M Na2MoO4, and 0.05% Triton X. Incubated Hsp90beta in a series dilution with 5 nM FITC-labeled geldanamycin for 150 minutes at room temperature. Fluorescence polarization measured at ex 470/em528.
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. Inhibition of Hsp90beta function has been shown to play a rolein tumorigenesis and disease progression.
Description: Human Heat Shock Protein 90β (GenBank Accession No. AY359878), full length with C-terminal His-tag, MW = 83 kDa, expressed in an E. coli expression system.
Format: Aqueous buffer solution
Formulation: 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl,2 mM DTT, and 20% glycerol.
Genbank: AY359878
Storage Stability: At least 6 months at -80°C.
Tags: C-terminal His-tag
Uniprot: P08238
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. Milicevic Z et al., Int J Oncol. 2008 Jun;32(6):1169-78.
2. Chao C.C. et al., J Cell Biochem. 2008 Jul 1;104(4):1286-96.
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