Recombinant full length Human Cu (I)-CCS (aa 1-274)(Copper chaperone for superoxide dismutase) with a GSFT sequence at N-terminal was expressed in E. coli. Binding of 2 Cu (I) to the protein was confirmed by ICP.
Copper chaperone for superoxide dismutase specifically delivers Cu to copper/zinc superoxide dismutase and may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
In 20 mM Phosphate buffer pH 7.0.
GMSF-MASDSGNQGT LCTLEFAVQM TCQSCVDAVR KSLQGVAGVQ DVEVHLEDQM VLVHTTLPSQ EVQALLEGTG RQAVLKMGS GQLQNLGAAV AILGGPGTVQ GVVRFLQLTP ERCLIEGTID GLEPGLHGLH VHQYGDLTMM CNSCGNHFNP DGASHGGPQD SDRHRGDLGN VRADADGRAI FRMEDEQLKV WDVIGRSLII DEGEDDLGRG GHPLSKITGN SGERLACGII ARSAGLFQNP KQICSCDGLT IWEERGRPIA GKGRKESAQP PAHL
>95% by SDS-PAGE. The protein was observed as a single band migrating at a molecular weight > 25 kDa and < 35 kDa.
To avoid oxidation and leaking of the Cu(I) bound to the protein, keep and use the sample under inert atomosphere.
Store at - 20 centigrade. The protein is stable at 4 centigrade for at least 2 weeks and at 25 centigrade for at least several hours. After initial deforst, aliquot product into individual tubes under inert atomosphere and refreeze at - 20 centigrade. Avoid repeated freeze/defrost cycles. Avoid exposition to air.