DnaJ homolog subfamily B member 11, APOBEC1-binding protein 2, ABBP-2, DnaJ protein homolog 9, ER-associated DNAJ, ER-associated Hsp40 co-chaperone, ER-associated dnaJ protein 3, ERdj3, ERj3p, HEDJ, Human DnaJ protein 9, hDj-9, PWP1-interacting protein 4, DNAJB11, EDJ, ERJ3, HDJ9, DJ9, Dj-9, ABBP2, UNQ537, PRO1080.

DNAJB11 is a member of the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJB11 serves as a co-chaperone for HSPA5 and binds directly to both unfolded proteins which are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed.

DNAJB11 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (23-358 a.a.) and having a molecular mass of 40.5kDa.
DNAJB11 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

MGSSHHHHHH SSGLVPRGSH MGRDFYKILG VPRSASIKDI KKAYRKLALQ LHPDRNPDDP QAQEKFQDLG AAYEVLSDSE KRKQYDTYGE EGLKDGHQSS HGDIFSHFFG DFGFMFGGTP RQQDRNIPRG SDIIVDLEVT LEEVYAGNFV EVVRNKPVAR QAPGKRKCNC RQEMRTTQLG PGRFQMTQEV VCDECPNVKL VNEERTLEVE IEPGVRDGME YPFIGEGEPH VDGEPGDLRF RIKVVKHPIF ERRGDDLYTN VTISLVESLV GFEMDITHLD GHKVHISRDK ITRPGAKLWK KGEGLPNFDN NNIKGSLIIT FDVDFPKEQL TEEAREGIKQ LLKQGSVQKV YNGLQGY.