Hsp27 (human recombinant)

Hsp27 (human recombinant)

CAT N°: 22736
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365.00 310.25

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).{40293,40294} 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.{40754} 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.{40295,40296,40297} Mutations in HSPB1 have been linked to hereditary neuromuscular diseases and cause Charcot-Marie-Tooth Disease Type 2 (CMT-2).{40298}

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