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Home Antibody All anti-HSPB1 antibodies

Anti-HSPB1 Antibody 5D12-A12

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Specifications Citations Related Products Product Documents
SKU Description Amount Price Availability*  
TA326365
  • Mouse monoclonal Hsp27 Antibody
  • FREE positive control: HEK293T cell transient overexpression lysate (LC400587) , 20ug
200µg 325 3-7 Days
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WB(1)
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Also for HSPB1 (NM_001540)
cDNA Clone shRNA/siRNA Lysate Protein Antibody

OriGene Data

ImmunogenHuman Hsp27
Clone Name5D12-A12 IsotypeIgG2b Kappa
Species ReactivityHuman. Very limited cross-reactivity to other species. Concentration1mg/mL
Guaranteed Application *WB Suggested DilutionsWB: 0.25-0.5 ug/ml
BufferPBS pH7.4, 50% glycerol
Purification Protein G Purified
Note Detects ~27kDa proteins corresponding to Hsp27 on SDS Page Immunoblots. Has no cross-reactivity to alphaB crystallin.

Reference Data

Target NameHomo sapiens heat shock 27kDa protein 1 (HSPB1)
Alternative NameCMT2F; HEL-S-102; HMN2B; HS.76067; Hsp25; HSP27; HSP28; SRP27
Database LinkNP_001531
FunctionHsp27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHsps is a homologous and highly conserved amino acid sequence, with an -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. Other functions include chaperone activity (as mentioned above), thermotolerance 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 .
Related Pathway
MAPK signaling pathway

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WB Image
Western blot analysis of Hsp27 in a variety of cells lines using a 1:1000 dilution of the antibody

 

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