CCS Antibody (H-7): sc-55561
- CCS Antibody (H-7) is a mouse monoclonal IgG1 κ CCS antibody, cited in 16 publications, provided at 200 µg/ml
- raised against amino acids 1-274 representing full length CCS of human origin
- CCS Antibody (H-7) is recommended for detection of CCS of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA
- Anti-CCS Antibody (H-7) is available conjugated to agarose for IP; HRP for WB, IHC(P) and ELISA; and to either phycoerythrin or FITC for IF, IHC(P) and FCM
- also available conjugated to Alexa Fluor® 488, Alexa Fluor® 546, Alexa Fluor® 594 or Alexa Fluor® 647 for WB (RGB), IF, IHC(P) and FCM, and for use with RGB fluorescent imaging systems, such as iBright™ FL1000, FluorChem™, Typhoon, Azure and other comparable systems
- also available conjugated to Alexa Fluor® 680 or Alexa Fluor® 790 for WB (NIR), IF and FCM; for use with Near-Infrared (NIR) detection systems, such as LI-COR®Odyssey®, iBright™ FL1000, FluorChem™, Typhoon, Azure and other comparable systems
- m-IgG Fc BP-HRP, m-IgG1 BP-HRP and m-IgGκ BP-HRP are the preferred secondary detection reagents for CCS Antibody (H-7) for WB and IHC(P) applications. These reagents are now offered in bundles with CCS Antibody (H-7) (see ordering information below).
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CCS Antibody (H-7) is a mouse monoclonal IgG1 kappa light chain antibody that detects CCS protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA). CCS (H-7) antibody is available in both non-conjugated and various conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates. The copper chaperone for superoxide dismutase-1 (CCS) plays a critical role in cellular antioxidant defense by facilitating the incorporation of copper into superoxide dismutase-1 (SOD-1), an enzyme essential for detoxifying harmful superoxide radicals. This process is vital because SOD-1 requires copper and zinc as cofactors to function effectively, and CCS ensures that copper is delivered specifically to SOD-1, preventing copper from binding to other intracellular copper-binding proteins that could disrupt cellular homeostasis. CCS is predominantly expressed in the kidney, liver, and Purkinje cells of the central nervous system, highlighting CCS′s importance in tissues that are particularly susceptible to oxidative stress. Furthermore, CCS exists as a homodimer and can form a heterodimer with SOD-1 during the copper loading process, which underscores CCS′s unique interaction with SOD-1 and significance in maintaining SOD-1′s activity and stability.
Alexa Fluor® is a trademark of Molecular Probes Inc., OR., USA
LI-COR® and Odyssey® are registered trademarks of LI-COR Biosciences
CCS Antibody (H-7) References:
- Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. | Rae, TD., et al. 1999. Science. 284: 805-8. PMID: 10221913
- Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. | Wong, PC., et al. 2000. Proc Natl Acad Sci U S A. 97: 2886-91. PMID: 10694572
- Cloning and mapping of murine superoxide dismutase copper chaperone (Ccsd) and mapping of the human ortholog. | Moore, SD., et al. 2000. Cytogenet Cell Genet. 88: 35-7. PMID: 10773661
- Mechanism of Cu,Zn-superoxide dismutase activation by the human metallochaperone hCCS. | Rae, TD., et al. 2001. J Biol Chem. 276: 5166-76. PMID: 11018045
- Heterodimer formation between superoxide dismutase and its copper chaperone. | Lamb, AL., et al. 2000. Biochemistry. 39: 14720-7. PMID: 11101286
- CCS and SOD1 mRNA are reduced after copper supplementation in peripheral mononuclear cells of individuals with high serum ceruloplasmin concentration. | Suazo, M., et al. 2008. J Nutr Biochem. 19: 269-74. PMID: 17683925
- Molecular and biochemical characterization of a unique mutation in CCS, the human copper chaperone to superoxide dismutase. | Huppke, P., et al. 2012. Hum Mutat. 33: 1207-15. PMID: 22508683
- Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase. | Levanon, D., et al. 1985. EMBO J. 4: 77-84. PMID: 3160582
- cDNA and deduced amino acid sequence of murine Cu-Zn superoxide dismutase. | Bewley, GC. 1988. Nucleic Acids Res. 16: 2728. PMID: 3362683
- The copper chaperone for superoxide dismutase. | Culotta, VC., et al. 1997. J Biol Chem. 272: 23469-72. PMID: 9295278
- The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. | Casareno, RL., et al. 1998. J Biol Chem. 273: 23625-8. PMID: 9726962
- The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain. | Rothstein, JD., et al. 1999. J Neurochem. 72: 422-9. PMID: 9886096
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
CCS Antibody (H-7) | sc-55561 | 200 µg/ml | $316.00 | |||
CCS Antibody (H-7): m-IgG Fc BP-HRP Bundle | sc-528601 | 200 µg Ab; 10 µg BP | $354.00 | |||
CCS Antibody (H-7): m-IgGκ BP-HRP Bundle | sc-521017 | 200 µg Ab, 40 µg BP | $354.00 | |||
CCS Antibody (H-7): m-IgG1 BP-HRP Bundle | sc-543020 | 200 µg Ab; 20 µg BP | $354.00 | |||
CCS Antibody (H-7) AC | sc-55561 AC | 500 µg/ml, 25% agarose | $416.00 | |||
CCS Antibody (H-7) HRP | sc-55561 HRP | 200 µg/ml | $316.00 | |||
CCS Antibody (H-7) FITC | sc-55561 FITC | 200 µg/ml | $330.00 | |||
CCS Antibody (H-7) PE | sc-55561 PE | 200 µg/ml | $343.00 | |||
CCS Antibody (H-7) Alexa Fluor® 488 | sc-55561 AF488 | 200 µg/ml | $357.00 | |||
CCS Antibody (H-7) Alexa Fluor® 546 | sc-55561 AF546 | 200 µg/ml | $357.00 | |||
CCS Antibody (H-7) Alexa Fluor® 594 | sc-55561 AF594 | 200 µg/ml | $357.00 | |||
CCS Antibody (H-7) Alexa Fluor® 647 | sc-55561 AF647 | 200 µg/ml | $357.00 | |||
CCS Antibody (H-7) Alexa Fluor® 680 | sc-55561 AF680 | 200 µg/ml | $357.00 | |||
CCS Antibody (H-7) Alexa Fluor® 790 | sc-55561 AF790 | 200 µg/ml | $357.00 |