Recombinant humaan DNAJB11-eiwit

DNAJB11 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. It serves as a co-chaperone for HSPA5 and 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. Recombinant human DNAJB11 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

DnaJ homolog subfamily B member 11, ABBP-2, ABBP2, DJ9, EDJ, ERdj3, ERj3, hDj9, HEDJ, PRO1080, uNQ537

E.coli

Human

His-Tag

SDS-PAGE

0.5 mg/mL (determined by Bradford assay)

> 90% by SDS-PAGE

40.5 kDa (357aa) confirmed by MALDI-TOF

DNAJB11, DnaJ homolog subfamily B member 11, ABBP-2, ABBP2, DJ9, EDJ, ERdj3, ERj3, hDj9, HEDJ, PRO1080, uNQ537, ATGP0985-10 µg, ATGP0985-20 µg, ATGP0985-50 µg, ATGP0985-100 µg, ATGP0985-250 µg, ATGP0985-500 µg, ATGP0985-1 mg, ATGP0985-10, ATGP0985-20, ATGP0985-50, ATGP0985-100, ATGP0985-250, ATGP0985-500, ATGP0985-1

Nakanishi K., et al. (2004) Cell Stress Chaperones. 9 (3) :253-64. ; ; Yu M., et al. (2000) J Biol Chem. 275 (32) :24984-92.

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol, 2mM DTT, 0.1M NaCl.

Heat Shock Proteins

NP_057390

Q9UBS4

Human

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