| Product Name | CCS, 1-274aa, Human |
|---|---|
| Description | 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. |
| Synonyms | Copper chaperone for superoxide dismutase, |
| Host | E. coli |
| Molecular Weight | 28.9kDa (256aa), confirmed by MALDI-TOF |
| Amino Acid Sequence | 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 |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol, 1mM DTT, 50mM NaCl |
| Concentration | 1mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Romerius P., et al. (2010) Clin Cancer Res. 16(15):3843-50. Seetharaman SV., et al. (2010) Biochemistry. 49(27):5714-25. |
| Background | 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. |
| Supplier | ARP |
All Research Products are sold for laboratory RESEARCH USE ONLY and ARE NOT TO BE USED FOR HUMAN OR ANIMAL THERAPEUTIC OR DIAGNOSTIC APPLICATIONS. The information presented is believed to be accurate; however, said information and products are offered without warranty or guarantee since the ultimate conditions of use and the variability of the materials treated are beyond our control. Nothing disclosed herein is to be construed as a recommendation to use our products in violation of any patents. ARP American Research Products, Inc. does not submit its products for regulatory review by any government body or other organization, and we do not validate them for clinical, therapeutic or diagnostic use, or for safety and effectiveness. You are solely responsible for making sure that the way you use the products complies with applicable laws, regulations and governmental policies and for obtaining all necessary approvals, intellectual property rights, licenses and permissions that you may need related to your use. Under no circumstances shall ARP American Research Products, Inc. be liable for damages, whether consequential, compensatory, incidental or special, strict liability or negligence, breach of warranty or any other theory arising out of the use of the products available from ARP American Research Products, Inc. Nothing contained herein warrants that the use of the products will not infringe on the claims of any patents covering the product itself or the use thereof in combination with other products or in the operation of any process. ARP American Research Products, Inc. disclaims any and all representations or warranties of any kind whatsoever, express or implied, including without limitation any implied warranties of merchantability or fitness for a particular purpose, of non-infringement, or regarding results obtained through the use of any product, whether arising from a statute or otherwise in law or from a course of performance, dealing or usage of trade.
