Hsp27 (human recombinant)

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).^1,2 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.³ 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.^4,5,6 Mutations in HSPB1 have been linked to hereditary neuromuscular diseases and cause Charcot-Marie-Tooth Disease Type 2 (CMT-2).⁷

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1. Hendrick, J.P., and Hartl, F.-U. Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384 (1993).

2. Schlesinger, M.J. Heat shock proteins. The Journal of Biological Chemisty 265(21), 12111-12114 (1990).

3. Carra, S., Alberti, S., Arrigo, P.A., et al. The growing world of small heat shock proteins: From structure to functions. Cell Stress Chaperones 22(4), 601-611 (2017).

4. Goloudina, A.R., Demidov, O.N., and Garrido, C. Inhibition of HSP70: A challenging anti-cancer strategy. Cancer Lett. 325(2), 117-124 (2012).

5. Kindås-Mügge, I., and Trautinger, F. Increased expression of the M_r 27,000 heat shock protein (hsp27) in in vitro differentiated normal human keratinocytes. Cell Growth Differ. 5(7), 777-781 (1994).

6. Rousseau, S., Houle, F., Kotanides, H., et al. 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. The Journal of Biological Chemisty 275(14), 10661-10672 (2000).

7. Evgrafov, O.V., Mersiyanova, I., Irobi, J., et al. Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. Nat. Genet. 36(6), 602-606 (2004).