HSP27
HSP27 (heat shock protein beta-1, encoded by HSPB1) is a small heat shock protein of the HSP20 family that acts as a molecular chaperone. It is also known as HSP28, Hsp25 and CMT2F, and contributes to stress resistance and actin organisation. Browse Assay Genie's current range of HSP27 research reagents below, or read on for the biology behind the target.
HSP27 is a small heat shock protein that functions as a molecular chaperone, probably maintaining denatured proteins in a folding-competent state. In response to environmental stress, the protein translocates from the cytoplasm to the nucleus, where it promotes the correct folding of other proteins. It plays a role in stress resistance and in actin organisation, and through its chaperone activity it may regulate numerous biological processes, including the phosphorylation and axonal transport of neurofilament proteins. HSP27 is also reported to play an important role in the differentiation of a wide variety of cell types.
The HSPB1 gene encodes heat shock protein beta-1, which belongs to the small heat shock protein (HSP20) family and is classified by HGNC within the small heat shock proteins gene group. UniProt records its locations as the cytoplasm, the nucleus and the spindle of the cytoskeleton. Mouse and rat each carry an ortholog named Hspb1, and the rodent protein is commonly referred to as Hsp25.
HSP27 has clear disease relevance. Expression of the gene is correlated with poor clinical outcome in multiple human cancers, and the protein may promote cancer cell proliferation and metastasis while protecting cancer cells from apoptosis. Mutations in the HSP27 gene have been identified in patients with Charcot-Marie-Tooth disease and distal hereditary motor neuropathy, which explains the CMT2F alias. Earlier names for the gene include heat shock 27kDa protein 1.
HSP27 is a chaperone that moves from cytoplasm to nucleus under environmental stress, making it a core readout for studying cellular stress resistance.
HSP27 expression correlates with poor clinical outcome in multiple cancers and may promote proliferation and metastasis while protecting cells from apoptosis.
Mutations in HSPB1 cause Charcot-Marie-Tooth disease and distal hereditary motor neuropathy, and HSP27 may influence neurofilament phosphorylation and axonal transport.
HSP27 contributes to actin organisation and to the differentiation of a wide variety of cell types, supporting cell biology studies.
HSP27 is a small heat shock protein that acts as a molecular chaperone, probably keeping denatured proteins in a folding-competent state. It contributes to stress resistance and actin organisation, and may regulate neurofilament phosphorylation and axonal transport. Under stress it moves from the cytoplasm to the nucleus.
The gene symbol is HSPB1, and the protein is named heat shock protein beta-1. Aliases include HSP27, HSP28, Hsp25 and CMT2F, and earlier names were heat shock 27kD protein 1 and heat shock 27kDa protein 1. HSP27 belongs to the small heat shock protein (HSP20) family.
Yes. Mutations in the HSP27 gene occur in patients with Charcot-Marie-Tooth disease and distal hereditary motor neuropathy, and its expression correlates with poor outcome in several cancers. Mouse and rat both have an ortholog named Hspb1; check the datasheet of any product for its validated reactivity.
Other small heat shock proteins and HSPB-associated targets relevant to chaperone, stress response and neuropathy research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P04792; product specifications from Assay Genie datasheets.