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| | Hsp27 (human recombinant) Basic information |
| | Hsp27 (human recombinant) Chemical Properties |
| | Hsp27 (human recombinant) Usage And Synthesis |
| Description | Heat shock protein 27 (Hsp27), also known as heat shock protein beta-1 (HspB1), is a member of the small heat shock protein (sHSP) family that is upregulated during conditions of cellular stress including heat shock, radiation, hypoxia, and exposure to reactive oxygen species (ROS). It is composed of an N-terminal domain, a highly conserved alpha-crystallin domain, and a C-terminal domain. Hsp27 functions as a molecular chaperone to prevent protein aggregation in an ATPase-independent manner. This chaperone activity is altered by changes in oligomerization state or by post-translational modifications including phosphorylation at serine residues 15 and 82, which increases affinity for damaged polypeptides in response to heat shock. Hsp27 also works in complex with other chaperone proteins, such as Hsp70 (Item Nos. 22739 | 23002), to correct misfolded proteins. This protein also plays a role in apoptosis, proteasome activation, cell differentiation, and has been shown to interact with actin and intermediate filaments. Mutations in HSPB1 have been linked to hereditary neuromuscular diseases and cause Charcot-Marie-Tooth Disease Type 2 (CMT-2). | | References | [1] J P HENDRICK F U H. Molecular chaperone functions of heat-shock proteins.[J]. Annual review of biochemistry, 1993, 62: 349-384. DOI: 10.1146/annurev.bi.62.070193.002025
[2] EDEN W, BROERE F, ZEE R. Heat Shock Proteins[C]. 1900: 0. DOI: 10.1007/978-3-7643-8550-7_94
[3] SERENA CARRA . The growing world of small heat shock proteins: from structure to functions[J]. Cell Stress & Chaperones, 2017, 22 4: Pages 601-611. DOI: 10.1007/s12192-017-0787-8
[4] ANASTASIA R. GOLOUDINA Carmen G Oleg N Demidov. Inhibition of HSP70: A challenging anti-cancer strategy[J]. Cancer letters, 2012, 325 2: Pages 117-124. DOI: 10.1016/j.canlet.2012.06.003
[5] I KINDS-MüGGE F T. Increased expression of the M(r) 27,000 heat shock protein (hsp27) in in vitro differentiated normal human keratinocytes.[J]. Cell growth & differentiation: the molecular biology journal of the American Association for Cancer Research, 1994, 5 7: 777-781.
[6] S ROUSSEAU. Vascular endothelial growth factor (VEGF)-driven actin-based motility is mediated by VEGFR2 and requires concerted activation of stress-activated protein kinase 2 (SAPK2/p38) and geldanamycin-sensitive phosphorylation of focal adhesion kinase.[J]. The Journal of Biological Chemistry, 2000, 275 14: 10661-10672. DOI: 10.1074/jbc.275.14.10661
[7] OLEG V EVGRAFOV. Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy[J]. Nature genetics, 2004, 36 6: 602-606. DOI: 10.1038/ng1354 |
| | Hsp27 (human recombinant) Preparation Products And Raw materials |
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