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Home / Primary Antibodies / Monoclonal Antibodies

HSP22 Antibody, Clone 3C12-H11 - SMC-187

BHA11901375
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Email
[email protected]
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Swissprot Q9UJY1
Accession Number NP_055180.1
Gene Id 26353
Target HSP22
Clone No 3C12-H11
Research Area Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Neurodegeneration, Neuroscience, Protein Trafficking
Buffer PBS pH7.4, 50% glycerol, 0.09% sodium azide
Concentration 1 mg/ml
Dilutions WB (1:2000), IHC (1:100); optimal dilutions for assays should be determined by the user.
Purification Protein G Purified
Scientific Background HSP27s 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 alpha-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 (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). 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), 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 (5). 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 (6).
Shipping Temperature Blue Ice or 4°C
Specificity Detects ~22kDa. Detects endogenous and exogenous HSP22 in monomeric, dimeric and tetrameric forms in WB. Does not cross react with alpha crystallin.
Storage -20ºC
Storage Buffer PBS pH7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Storage Temperature -20°C
Applications ELISA, IHC, WB, ICC/IF
Description WB ; IHC ; ICC ; IF ; ELISA
Dilution WB (1:2000), IHC (1:100); optimal dilutions for assays should be determined by the user.
Product Manual SDS
SDS
Reference 1.Kappe G., et al. (2001) Biochem Biophys Acta 1520: 1-6.

2. Benndorf R., et al. (2001) J Biol Chem 276: 26753-26761.

3.Sun X., et al. (2004) J Biol Chem 279: 2394-2402.

4.Kim M.V., et al. (2004) Biochem Biophys Res Commun 325: 649-652.

5. Wilhelmus M.M., et al. (2006)Acta Neuropathol (Berl) 111: 139-149.
Combination SKU Supplier No. Conjugate Size Your price Quantity
BHA11901375-1 SMC-187D Unconjugated 100 ug $330
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BHA11901375-2 SMC-187C Unconjugated 25 ug $179
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BHA11901375-3 SMC-187D-A390 ATTO 390 100 ug $384
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BHA11901375-4 SMC-187D-A488 ATTO 488 100 ug $383
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BHA11901375-5 SMC-187D-A594 ATTO 594 100 ug $383
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BHA11901375-6 SMC-187D-ALP Alkaline Phosphatase 100 ug $376
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BHA11901375-7 SMC-187D-APC APC 100 ug $382
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BHA11901375-8 SMC-187D-BI Biotin 100 ug $378
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BHA11901375-9 SMC-187D-FITC FITC 100 ug $374
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BHA11901375-10 SMC-187D-HRP HRP 100 ug $370
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BHA11901375-11 SMC-187D-PCP PerCP 100 ug $382
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BHA11901375-12 SMC-187D-RPE RPE 100 ug $380
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BHA11901375-13 SMC-187S Unconjugated 12 ug $44
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