anti-HSP27 (Phospho-Ser82), mAb (41A8)

CHF 322.00
In stock
YIF-LF-MA0285100 µlCHF 322.00
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Product Details
Synonyms Phospho-HspB1; Phospho-HSP27; Phospho-SRP27; Phospho-HSPB1; Phospho-HSP 27; Phospho-Heat Shock Protein β-1; Phospho-Heat Shock 27 kDa Protein; Phospho-28 kDa Heat Shock Protein
Product Type Monoclonal Antibody
Properties
Clone 41A8
Isotype Mouse IgG1 κ
Immunogen/Antigen Synthetic phospho-peptide.
Application

ELISA
Western Blot (1:5,000)
Immunoprecipitation (2 μl)

Crossreactivity Human
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
Documents
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF

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, α-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 approximately 27 kDa, although it has been shown to form large aggregates of up to 800 kDa 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. Involved in stress resistance and actin organization.

Product References

1) So A et al. (2007) Curr Genomics. 8(4):252-261 (General)
2) Ferns G et al. (2006) Int J Exp Pathol. 87(4):253-274 (General)
3) Ciocca DR and Calderwood SK, (2005) Cell Stress Chaperones. 10(2):86-103. (General)

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