|Other Names||DnaJ homolog subfamily B member 11, APOBEC1-binding protein 2, ABBP-2, DnaJ protein homolog 9, ER-associated DNAJ, ER-associated Hsp40 co-chaperone, Endoplasmic reticulum DNA J domain-containing protein 3, ER-resident protein ERdj3, ERdj3, ERj3p, HEDJ, Human DnaJ protein 9, hDj-9, PWP1-interacting protein 4, DNAJB11, EDJ, ERJ3, HDJ9|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||EDJ, ERJ3, HDJ9|
|Function||Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity.|
|Cellular Location||Endoplasmic reticulum lumen Note=Associated with the ER membrane in a C-terminally epitope- tagged construct|
|Tissue Location||Widely expressed.|
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DNAJB11 belongs to the evolutionarily conserved DNAJ/HSP40family of proteins, which regulate molecular chaperone activity bystimulating ATPase activity. DNAJ proteins may have up to 3distinct domains: a conserved 70-amino acid J domain, usually atthe N terminus; a glycine/phenylalanine (G/F)-rich region; and aC-terminal cysteine-rich region (Ohtsuka and Hata, 2000 [PubMed11147971]).
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Wen, K.W., et al. Oncogene 29(24):3532-3544(2010)Bernal-Bayard, J., et al. J. Biol. Chem. 285(21):16360-16368(2010)Vembar, S.S., et al. J. Biol. Chem. 284(47):32462-32471(2009)Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
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