HSPB8

HSPB8

Target · Small heat shock protein

HSPB8 Heat shock protein family B (small) member 8 · Heat shock protein beta-8

HSPB8 (heat shock protein family B (small) member 8, also known as H11, E2IG1, HSP22 and CMT2L) is a small heat shock protein of the HSP20 family. It acts as a chaperone and takes part in chaperone-assisted selective autophagy, a protein quality control pathway. Browse Assay Genie's current range of HSPB8 research reagents below, or read on for the biology behind the target.

Cytoplasm and nucleusChaperone, HSP20 familyLinked to neuromuscular disease
196 aa
Protein length
~22 kDa
Molecular weight
12q24.23
Gene locus
HSP20 family
Protein family
Target information

What is HSPB8 (heat shock protein family B (small) member 8)?

HSPB8 is involved in chaperone-assisted selective autophagy (CASA), a process that is crucial for protein quality control, particularly in cells and tissues under mechanical strain, such as muscle. The protein displays temperature-dependent chaperone activity. According to the NCBI Gene summary, it also functions as a chaperone in association with Bag3, a stimulator of macroautophagy.

The HSPB8 gene encodes a member of the superfamily of small heat shock proteins, which share a conserved alpha-crystallin domain at the C-terminal part of the molecule. HGNC places it in the small heat shock proteins gene group, and UniProt assigns it to the small heat shock protein (HSP20) family. The protein is found in the cytoplasm and the nucleus. Expression of the gene is induced by oestrogen in oestrogen receptor-positive breast cancer cells.

The gene was formerly named heat shock 27kDa protein 8 and heat shock 22kDa protein 8, and it is also known as H11, E2IG1, HSP22 and CMT2L. Its link to autophagy and its oestrogen-induced expression suggest a role in the regulation of cell proliferation, apoptosis and carcinogenesis. Mutations in the gene have been associated with several neuromuscular diseases, including Charcot-Marie-Tooth disease. Mouse and rat orthologs are both designated Hspb8, which allows the protein to be studied in common rodent models.

Autophagy and proteostasis

HSPB8 contributes to chaperone-assisted selective autophagy, making it a useful target for studying protein quality control in mechanically strained tissues.

Neuromuscular disease research

Mutations in HSPB8 are associated with neuromuscular diseases including Charcot-Marie-Tooth disease, so it is studied in models of nerve and muscle disorders.

Cancer biology

HSPB8 is oestrogen-induced in oestrogen receptor-positive breast cancer cells and appears to be involved in proliferation, apoptosis and carcinogenesis.

Chaperone and stress biology

As a small heat shock protein with temperature-dependent chaperone activity, HSPB8 is relevant to studies of cellular stress responses and Bag3 partnership.

Background

HSPB8 frequently asked questions

What does HSPB8 do?

HSPB8 is a small heat shock protein with temperature-dependent chaperone activity. It is involved in chaperone-assisted selective autophagy, an important protein quality control process in mechanically strained tissues such as muscle, and it works with the macroautophagy stimulator Bag3.

What other names is HSPB8 known by?

HSPB8 is also called H11, E2IG1, HSP22 and CMT2L. Earlier names were heat shock 27kDa protein 8 and heat shock 22kDa protein 8. UniProt lists the protein as heat shock protein beta-8, and HGNC places it in the small heat shock proteins group.

Is HSPB8 linked to disease, and is it conserved in rodents?

Mutations in HSPB8 have been associated with neuromuscular diseases, including Charcot-Marie-Tooth disease. Mouse and rat both have an ortholog named Hspb8, so rodent models can be used for study. Check the datasheet of any product for its validated reactivity.

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Related targets

Other small heat shock proteins and HSPB-associated targets with products at Assay Genie.

Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9UJY1; product specifications from Assay Genie datasheets.

HSPB8 Product listing