Heat shock proteins are ubiquitous proteins and have been characterized as cytoprotective molecular chaperones. The typical function of a chaperone is to assist a protein to attain its functional conformation to prevent non-functional aggregation of misfolded proteins. The principal HSP families are HSP90, HSP70, HSP60 and the small HSPs including HSP27, ubiquitin, alpha-crystallin, Hsp20 and others. The common functions of small Hsps are chaperone activity, thermotolerance, inhibition of apoptosis, regulation of cell development, and cell differentiation. Hsp27 has a molecular weight of ~27kD, although it has been shown to form large aggregates of up to 800kD in the cytosol. Hsp27 is found in several types of human cells, including tumour cells. Hsp27 interferes with apoptosis through its ability to interact with and inhibit key components of the apoptotic signaling pathway, including the caspase activation complex. Overexpression of heat shock proteins can increase the tumorigenic potential of tumour cells. HSP27 also has been reported to be involved in development and progression of hormone-refractory prostate cancer.
Source:
Recombinant corresponding to aa1-205 from human HSP27, fused to N-His tag expressed in E.coli.
Molecular Weight:
~25kD
Storage and Stability:
Aliquot to avoid repeated freezing and thawing and store at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
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