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-terminal domain, was expressed in E.coli and purified by using conventional chromatography techniques.||Source:|Recombinant protein corresponding to aa1-274 from human CCS, fused to His-tag at N-terminal domain, expressed in E.coli.||Molecular Weight:|~31.2kD (MALDI-TOF)||Applications:|Suitable for use in SDS-PAGE. Other applications not tested.||Recommended Dilution:|Optimal dilutions to be determined by the researcher.||AA Sequence:|MGSSHHHHHHSSGLVPRGSHMASDSGNQGTLCTLEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLEDQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGSGQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTIDGLEPGLHGLHVHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAIFRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGIIARSAGLFQNPKQICSCDGLTIWEEGRPIAGKGRKESAQPPAHL||Storage and Stability:|May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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