DNAJB2
DNAJB2 (DnaJ heat shock protein family (Hsp40) member B2, also known as HSJ1, HSPF3 and CMT2T) is a member of the DNAJ (HSP40) heat shock protein group. It acts as a co-chaperone for HSP70 family chaperones and contributes to the handling of misfolded proteins. Browse Assay Genie's current range of DNAJB2 research reagents below, or read on for the biology behind the target.
DNAJB2 functions as a co-chaperone. It regulates substrate binding and activates the ATPase activity of chaperones of the HSP70 (heat shock protein 70) family. In parallel, the DNAJB2 protein contributes to the ubiquitin-dependent proteasomal degradation of misfolded proteins. Through these activities it may regulate the aggregation, and promote the functional recovery, of misfolded proteins such as HTT, MC4R, PRKN, RHO and SOD1, and it may be crucial for many biological processes.
The DNAJB2 gene is almost exclusively expressed in the brain, mainly in the neuronal layers. The encoded protein shows sequence similarity to bacterial DnaJ and its yeast homologues; in bacteria, DnaJ is implicated in protein folding and protein complex dissociation. Alternatively spliced transcript variants encoding different isoforms have been described. Isoform 1 is localised to endoplasmic reticulum membranes and may specifically function in ER-associated degradation of misfolded proteins. UniProt lists the protein in the cytoplasm, nucleus and endoplasmic reticulum membrane.
DNAJB2 is also known as HSJ1 and HSPF3, and the symbol CMT2T is among its aliases. Its previous HGNC name was DnaJ (Hsp40) homolog, subfamily B, member 2. A mouse ortholog, Dnajb2, is recognised. Because of its role in the clearance and aggregation control of misfolded substrates, DNAJB2 is a useful subject for studies of protein quality control in neurons.
DNAJB2 couples HSP70 chaperone activity to ubiquitin-dependent proteasomal degradation of misfolded proteins, making it a focus for proteostasis research.
DNAJB2 may regulate aggregation of misfolded substrates including HTT, PRKN, RHO and SOD1, relevant to models of protein misfolding.
Isoform 1 localises to the endoplasmic reticulum membrane and may function specifically in ER-associated degradation of misfolded proteins.
The gene is almost exclusively expressed in the brain, mainly in neuronal layers, supporting its study in neuronal chaperone function.
DNAJB2 is a co-chaperone that regulates substrate binding and activates the ATPase activity of HSP70 family chaperones. It also contributes to ubiquitin-dependent proteasomal degradation of misfolded proteins, and may regulate aggregation and promote functional recovery of substrates such as HTT, MC4R, PRKN, RHO and SOD1.
DNAJB2 is also called HSJ1, HSPF3 and CMT2T, and was previously named DnaJ (Hsp40) homolog, subfamily B, member 2. Alternatively spliced transcript variants encode different isoforms. Isoform 1 localises to endoplasmic reticulum membranes and may act in ER-associated degradation of misfolded proteins.
The DNAJB2 gene is almost exclusively expressed in the brain, mainly in the neuronal layers. Its protein resembles bacterial DnaJ and yeast homologues, and a mouse ortholog, Dnajb2, exists. Check the datasheet of any product for its validated reactivity.
Other DNAJ (HSP40) co-chaperones and related heat shock proteins involved in protein folding and quality control.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P25686; product specifications from Assay Genie datasheets.