Heat Shock 22kDa Protein 8 (HSPB8) antibody

Details for Product No. ABIN361851, Supplier: Log in to see
Antigen
  • MGC64408
  • fc09c11
  • wu:fc04b04
  • wu:fc09c11
  • zgc:64202
  • CMT2L
  • DHMN2
  • E2IG1
  • H11
  • HMN2
  • HMN2A
  • HSP22
  • AU018630
  • AW413033
  • Cryac
  • D5Ucla4
  • H11K
  • HSP20-like
  • Hsp22
  • heat shock 22kDa protein 8
  • heat shock protein, alpha-crystallin-related, b8
  • heat shock protein 8
  • heat shock protein B8
  • hspb8
  • HSPB8
  • LOC100349029
  • Hspb8
Reactivity
Human, Mouse (Murine), Rat (Rattus)
153
93
90
5
5
4
4
4
2
2
2
1
1
1
1
Host
Rabbit
80
64
9
Clonality
Polyclonal
Conjugate
Un-conjugated
7
7
4
4
4
3
3
3
3
3
3
3
3
3
3
3
2
1
1
1
1
1
1
1
1
1
1
1
1
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
126
89
73
67
48
23
16
13
7
5
2
2
1
1
1
1
1
Options
Supplier
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Immunogen Human HSP22
Specificity Detects ~22 kDa. Does not cross-react with HSP27 or alpha-crystallin.
Purification Peptide Affinity Purified
Alternative Name HSP22 (HSPB8 Antibody Abstract)
Background HSP22 (HSPB8) is a 196-amino acid protein that is a member of the small heat shock protein super-family and the human protein is most closely related to HSP27. Similar to most other sHSPs, HSP22 is predominately transcribed in skeletal muscle and heart, as well as the placenta (1). HSP22 is a monomeric protein which interacts with HSPB1. It displays temperature-dependent chaperone activity. In a two hybrid screen, HSPB8 interacted preferentially with a triple aspartate form of HSP27 which mimics HSP27 phosphorylated at Ser15, Ser78, and Ser82, as compared to wild-type HSP27 (2). HSPB8 has two binding domains (N and C Terminal) that are specific for different binding partners, and has the ability to bind itself and other sHSPs (3). The chaperone-like activity is of great importance to the function of HSP22 in various processes including proliferation, apoptosis and macro autophagy (4). Mutations in the HSPB8 gene are associated with the inherited peripheral neuropathies, autosomal dominant distal hereditary motor neuropathy type IIA (dSMA) and axonal Charcot-Marie-Tooth disease type 2L (CMT2L) (5).
Gene ID 26354
NCBI Accession NP_055180
UniProt Q9UJY2
Application Notes
  • WB (1:1000)
  • ICC/IF (1:100)
  • IHC (1:100)
  • optimal dilutions for assays should be determined by the user.
Comment

A 1:1000 dilution of SPC-181 was sufficient for detection of HSP22 in 10 μg of rat tissue lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Storage -20 °C
Supplier Images
 image for anti-Heat Shock 22kDa Protein 8 (HSPB8) antibody (ABIN361851) Hsp22, Mouse Spinal Cord
Background publications Wilhelmus, Boelens, Otte-Höller, Kamps, Kusters, Maat-Schieman, de Waal, Verbeek: "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, Shelden, Welsh, Benndorf: "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).

Benndorf, Sun, Gilmont, Biederman, Molloy, Goodmurphy, Cheng, Andrews, Welsh: "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).

Kappé, Verschuure, Philipsen, Staalduinen, Van de Boogaart, Boelens, De Jong: "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).