Recombinant humaan CCS-eiwit

CCS is essential for the incorporation of copper into SOD-1, and therefore is necessary for its enzymatic activity. CCS prevents copper ions from binding to intracellular copper scavengers and provides the SOD-1 enzyme with the necessary copper cofactor. CCS escorts copper only to SOD-1 and fails to deliver copper to proteins in the mitochondria, nucleus or secretory pathway. While many tissues express CCS, the chaperone is most abundant in the kidney, liver and Purkinje cells in the neuropil of the central nervous system. Recombinant human CCS protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

Copper chaperone for superoxide dismutase

E.coli

Human

His-Tag

SDS-PAGE

1 mg/mL (determined by Bradford assay)

> 90% by SDS-PAGE

31.2 kDa (294aa) confirmed by MALDI-TOF

CCS, Copper chaperone for superoxide dismutase, ATGP0715-10 µg, ATGP0715-20 µg, ATGP0715-50 µg, ATGP0715-100 µg, ATGP0715-250 µg, ATGP0715-500 µg, ATGP0715-1 mg, ATGP0715-10, ATGP0715-20, ATGP0715-50, ATGP0715-100, ATGP0715-250, ATGP0715-500, ATGP0715-1

Romerius P., et al. (2010) Clin Cancer Res. 16 (15) :3843-50.; ; Seetharaman SV., et al. (2010) Biochemistry. 49 (27) :5714-25.;

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 0.2M NaCl 1mM DTT, 10% glycerol

Cancer

NP_005116

O14618

Human

MASDSGNQGT LCTLEFAVQM TCQSCVDAVR KSLQGVAGVQ DVEVHLEDQM VLVHTTLPSQ EVQALLEGTG RQAVLKGMGS GQLQNLGAAV AILGGPGTVQ GVVRFLQLTP ERCLIEGTID GLEPGLHGLH VHQYGDLTNN CNSCGNHFNP DGASHGGPQD SDRHRGDLGN VRADADGRAI FRMEDEQLKV WDVIGRSLII DEGEDDLGRG GHPLSKITGN SGERLACGII ARSAGLFQNP KQICSCDGLT IWEERGRPIA GKGRKESAQP PAHL