CCS protein (His tag) (80R-1477)
Purified recombinant Human CCS protein
|Synonyms||Copper chaperone for superoxide dismutase protein,|
Coomassie Blue stained SDS-PAGE of CCS protein (His tag) (80R-1477)
Figure annotation denotes ug of protein loaded and % gel used.
|Residues||1-274 amino acids: MGSSHHHHHH SSGLVPRGSH 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|
|Purity||> 90% pure|
|Molecular Weight||31.2 kDa (294aa), confirmed by MALDI-TOF|
|Form & Buffer||Supplied as a liquid in 20mM Tris-HCl buffer, pH 8.0, containing 0.2M NaCl, 1mM DTT and 10% glycerol.|
Storage & Safety
|Storage||Store at 4 deg C for short term storage (1/2 weeks). Aliquot and store at -20 deg C or - 70 deg C for long term storage. Avoid repeated freeze/thaw cycles.|
|Biological Significance||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.|
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