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Heat Shock 22kDa Protein 8 (HSPB8) antibody

Details for Product No. ABIN863103, Supplier: Log in to see
  • MGC64408
  • fc09c11
  • wu:fc04b04
  • wu:fc09c11
  • zgc:64202
  • CMT2L
  • DHMN2
  • E2IG1
  • H11
  • HMN2
  • HMN2A
  • HSP22
  • AU018630
  • AW413033
  • Cryac
  • D5Ucla4
  • H11K
  • HSP20-like
  • Hsp22
Human, Mouse (Murine), Rat (Rattus)
Clonality (Clone)
Monoclonal ()
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
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Immunogen His-tagged human recombinant HSP22
Clone 3C12-H11
Specificity Detects ~22 kDa. Detects endogenous and exogenous HSP22 in monomeric, dimeric and tetrameric forms in WB. Does not cross react with alpha crystallin.
Sensitivity 1 µg/mL of SMC-187 was sufficient for detection of Hsp22 in 20 µg of whole rat tissue extract by ECL immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
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 α-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).
Cellular Localization: Cytoplasm | Nucleus
Gene ID 26353
NCBI Accession NP_055180
UniProt Q9UJY1
Application Notes Recommended Dilution: WB (1:2000), IHC (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-Heat Shock 22kDa Protein 8 (HSPB8) antibody (ABIN863103) HSP22 (3C12 H11), Mouse backskin.
Western Blotting (WB) image for anti-Heat Shock 22kDa Protein 8 (HSPB8) antibody (ABIN863103) Rat tissue Mix WB 1 in 1000 Hsp22 monomer and dimer.
Background publications Wilhelmus, Boelens, Otte-Höller et al.: "Small heat shock protein HspB8: its distribution in Alzheimer's disease brains and its inhibition of amyloid-beta protein aggregation and cerebrovascular amyloid-beta toxicity." in: Acta neuropathologica, Vol. 111, Issue 2, pp. 139-49, 2006 (PubMed).

Kim, Seit-Nebi, Gusev: "The problem of protein kinase activity of small heat shock protein Hsp22 (H11 or HspB8)." in: Biochemical and biophysical research communications, Vol. 325, Issue 3, pp. 649-52, 2004 (PubMed).

Sun, Fontaine, Rest et al.: "Interaction of human HSP22 (HSPB8) with other small heat shock proteins." in: The Journal of biological chemistry, Vol. 279, Issue 4, pp. 2394-402, 2004 (PubMed).

Kappé, Verschuure, Philipsen et al.: "Characterization of two novel human small heat shock proteins: protein kinase-related HspB8 and testis-specific HspB9." in: Biochimica et biophysica acta, Vol. 1520, Issue 1, pp. 1-6, 2001 (PubMed).

Benndorf, Sun, Gilmont et al.: "HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27)." in: The Journal of biological chemistry, Vol. 276, Issue 29, pp. 26753-61, 2001 (PubMed).