Anti-Human Hsp27 DyLight® 488 conjugated HSPB1 Antibody(monoclonal, 3H3), Carrier-free

HSPB1 (Heat shock 27kDa protein 1), also known as HSP27, is a protein that in humans is encoded by the HSPB1 gene. HSP27 gene is mapped to 7q11.23. The protein encoded by this gene is induced by environmental stress and developmental changes. The encoded protein is involved in stress resistance and actin organization and translocates from the cytoplasm to the nucleus upon stress induction. Defects in this gene are a cause of Charcot-Marie-Tooth disease type 2F (CMT2F) and distal hereditary motor neuropathy (dHMN).

Heat shock protein beta-1; HspB1; 28 kDa heat shock protein; Estrogen-regulated 24 kDa protein; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; HSPB1; HSP27; HSP28

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742).

1. Ackerley, S., James, P. A., Kalli, A., French, S., Davies, K. E., Talbot, K. A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes. Hum. Molec. Genet. 15: 347-354, 2006. 2. d'Ydewalle, C., Krishnan, J., Chiheb, D. M., Van Damme, P., Irobi, J., Kozikowski, A. P., Vanden Berghe, P., Timmerman, V., Robberecht, W., Van Den Bosch, L. HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1-induced Charcot-Marie-Tooth disease. Nature Med. 17: 968-974, 2011. 3. Stock, A. D., Spallone, P. A., Dennis, T. R., Netski, D., Morris, C. A., Mervis, C. B., Hobart, H. H. Heat shock protein 27 gene: chromosomal and molecular location and relationship to Williams syndrome. Am. J. Med. Genet. 120A: 320-325, 2003.

Nucleus. Nucleus, nucleolus. Nucleus speckle. Endoplasmic reticulum. Cytoplasm. Detected in the cytoplasm of B-cells stimulated to switch (By similarity). Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm. .