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HSP25 (mouse), (recombinant)

ADI-NSP-510-F 200 µg 546.00 USD
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Product Specification

Alternative Name:HspB1, Heat shock protein 25
Source:Produced in E. coli.
UniProt ID:P14602
GenBank ID:L07577
Formulation:Liquid. In Dulbecco's PBS.
Purity:≥90% (SDS-PAGE; Western blot)
Purity Detail:Purified by multi-step chromatography.
Endotoxin Content:>500EU/mg purified protein (LAL test)
Kinase assay
Application Notes:Western blot control.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Scientific Background:Mouse Hsp25, human Hsp27, and αβ-crystallin are part of a diverse family of small heat shock proteins (sHsps) which are produced in all organisms. The overall homology between the different sHsps is low and they are grouped together based on conserved sequences in the C-terminal half of the protein and short conserved phenylalanine-rich stretches near the N terminus. Mammalian sHsps are expressed constitutively under physiological conditions but stress factors such as heat shock induce a strong up-regulation of protein levels by 10-20-fold to maximum concentrations of 0.1% of the cellular protein. They function as chaperone-like proteins by binding unfolded polypeptides and preventing uncontrolled protein aggregation. sHsps all share the striking feature of forming high molecular weight oligomeric complexes of variable size. The quaternary structure of sHsps is essential for their function and regulation of activity but its basic properties are still rather poorly understood. Data indicates that Hsp25 is a dynamic tetramer of tetramers with a unique ability to refold and reassemble into its active quaternary structure after denaturation. Current studies demonstrate that Hsp25 helps facilitate the glutathione-redox cycle by enhancing glutathione utilization and maintaining the cellular glutathione pool in favor of the reduced states.

Product Literature References

Innervation-dependent phosphorylation and accumulation of alphaB-crystallin and Hsp27 as insoluble complexes in disused muscle: Y. Inaguma, et al. ; FASEB J. 16, 1432 (2002), Application(s): WB using mouse samples, Abstract;
An N-terminal 33-amino-acid-deletion variant of hsp25 retains oligomerization and functional properties: L.F. Cooper, et al. ; Biochem. Biophys. Res. Commun. 270, 183 (2000), Application(s): Other using mouse samples, Abstract;

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