DNAJB11 Human
Description
DNAJB11 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
DnaJ (Hsp40) Homolog, Subfamily B, Member 11, also known as DNAJB11, is a member of the DnaJ/Hsp40 family of proteins. These proteins play a crucial role in regulating molecular chaperone activity by stimulating ATPase activity. DNAJB11 is a soluble glycoprotein located in the endoplasmic reticulum (ER) and acts as a co-chaperone for GRP78 (HSPA5), a heat shock protein chaperone essential for the proper folding, assembly, trafficking, and degradation of proteins .
The DNAJB11 gene is located on chromosome 3q27.3 and encodes a protein consisting of 358 amino acids . The protein contains several distinct domains, including a conserved 70-amino acid J domain at the N-terminus, a glycine/phenylalanine (G/F)-rich region, and a C-terminal cysteine-rich region . These domains are characteristic of the DnaJ/Hsp40 family and are essential for the protein’s function in molecular chaperoning.
DNAJB11 functions as a co-chaperone for GRP78, assisting in the proper folding, trafficking, or degradation of proteins within the ER . It binds directly to both unfolded proteins that are substrates for ER-associated degradation (ERAD) and nascent unfolded peptide chains. DNAJB11 dissociates from the GRP78-unfolded protein complex before the folding process is completed . This interaction is crucial for maintaining ER protein homeostasis and preventing the accumulation of misfolded proteins, which can lead to cellular stress and disease.
DNAJB11 is expressed in various tissues, with the highest expression levels observed in the pancreas and testis . It is localized to the endoplasmic reticulum, where it performs its co-chaperone functions. The protein is luminally oriented and membrane-associated, as demonstrated by protease susceptibility, glycosidase treatment, and detergent solubility assays .
Mutations or dysregulation of DNAJB11 have been associated with certain diseases, including polycystic kidney disease 6 with or without polycystic liver disease . The protein’s role in maintaining ER protein homeostasis highlights its importance in cellular function and its potential as a therapeutic target for diseases related to protein misfolding and ER stress.
