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Anti-HSPB2 Antibody 8A7
Also for HSPB2 (NM_001540)
|Mouse, Rat, Bovine, Canine, Guinea pig, Hamster. Recognizes Hsp25 and Hsp27, cross reacts with alpha B crystallin.
||WB 1:5000 (ECL), 1:200 (IF)
|PBS, 50% glycerol|
|Protein G Purified
|Detects an 25kDa or 27kDa protein corresponding to the molecular mass of Hsp25/27 on SDS PAGE immunoblots.
|Homo sapiens heat shock 27kDa protein 1 (HSPB1)|
|CMT2F; HEL-S-102; HMN2B; HS.76067; Hsp25; HSP27; HSP28; SRP27|
|Hsp25 is the mouse homologue of the human Hsp27 protein, a member of the small heat shock protein family comprised of a diverse group of proteins from ~15 to >30kDa. The basic structure of most sHsps is a homologous and highly conserved amino acid sequence, with an a-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers . Hsp27-oligomers consist of stable dimers formed by as many as 8-40 Hsp27 protein monomers . The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity .HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. It can be rapidly phosphorylated in response to physiological stimuli relevant to the cell type examined. Thus, hsp27 has been suggested to be an important intermediate in second messenger-mediated signaling pathways . Other functions include chaperone activity (as mentioned above), thermo-tolerance in vivo, inhibition of apoptosis, and signal transduction.Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. Hsp27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that hsp27 may serve some role in cross-bridge formation between actin and myosin . And finally, Hsp27 is also thought to be involved in the process of cell differentiation. The up-regulation of Hsp27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that Hsp27 may play a crucial role in termination of growth .|
MAPK signaling pathway
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Western blot analysis of Hsp25/27 in rat lung tissues, using a 1:1000 dilution of the antibody
Somites of a rat embryo at 11 days of gestation. Red is rhodamine-phalloidin labeled actin and green is Hsp27. Courtesy of Mike Welsh, University of Michigan.