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DNAJB12 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. Additionally we are shipping DNAJB12 Antibodies (54) and DNAJB12 Proteins (5) and many more products for this protein.
Data suggest that endoplasmic reticulum (ER) stress-induced apoptosis in hepatoma cells is regulated by highly labile and ER-associated BCL-2 (show BCL2 ELISA Kits) family member BOK (show BOK ELISA Kits), which is controlled at level of protein stability by ER-associated degradation components; DNAJB12 is required in hepatoma cells to maintain BOK (show BOK ELISA Kits) at low levels and suppress ER stress. (DNAJB12 = DnaJ (Hsp40 (show DNAJB1 ELISA Kits)) homolog (show DNAJB4 ELISA Kits), subfamily B (show CYP ELISA Kits), member 12)
Over-expression of DNAJB12 or DNAJB14 (show DNAJB14 ELISA Kits) causes the formation of elaborate membranous structures within cell nuclei, designated DJANGOS for DNAJ (show DNAJB6 ELISA Kits)-associated nuclear globular structures.
JB12 cooperates with cytosolic Hsc70 (show HSPA8 ELISA Kits) and the ubiquitin ligase RMA1 to target CFTR (show CFTR ELISA Kits) and CFTRDeltaF508 for degradation.
DNAJB12 is a novel mammalian ER-localized J-protein that plays a vital role in the quality control of membrane proteins
DNAJB12 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus\; a glycine/phenylalanine (G/F)-rich region\; and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain (Ohtsuka and Hata, 2000
DnaJ (Hsp40) homolog, subfamily B, member 12
, dnaJ homolog subfamily B member 12
, dnaJ homolog subfamily B member 12-like
, DnaJ homolog 10