Application
| WB, IHC, ICC |
---|---|
Primary Accession | Q9UJY2 |
Other Accession | NP_055180.2 |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Clonality | Polyclonal |
Description | Rabbit Anti-Human HSP22 Polyclonal |
Target/Specificity | Detects ~22kDa. Does not cross-react with HSP27 or alpha-crystallin. |
Other Names | Alpha crystallin C chain Antibody, CMT2L Antibody, CRYAC Antibody, DHMN2 Antibody, H11 Antibody, Heat shock 22kDa protein 8 Antibody, HMN2 Antibody, HSB8 Antibody, HSPB8 Antibody |
Immunogen | Human HSP22 |
Purification | Peptide Affinity Purified |
Storage | -20ºC |
Storage Buffer | PBS pH7.4, 50% glycerol, 0.09% sodium azide |
Shipping Temperature | Blue Ice or 4ºC |
Certificate of Analysis | 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. |
Cellular Localization | Cytoplasm | Nucleus |
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Provided below are standard protocols that you may find useful for product applications.
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).
References
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.