SOD4 (CCS, Copper chaperone for superoxide dismutase, Superoxide Dismutase 4) (Internal Region) antibody

Antigen: SOD4 (CCS, Copper chaperone for superoxide dismutase, Superoxide Dismutase 4)

Binding Site: Internal Region

Clonality: Polyclonal

Host: Rabbit

Application: Immunohistochemistry (IHC), Western Blotting (WB)

Catalog no.: ABIN350845

Additional Information

UniProt: O14618

Immunogen: A synthetic peptide from the internal part of human SOD4 (CCS, Copper chaperone for superoxide dismutase, Superoxide Dismutase 4) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen shares 95% and 92% identity with mouse and rat sequence respectively.

Format: Lyophilized

Description: Function: Delivers copper to copper zinc superoxide dismutase (SOD1). Subcellular location: Cytoplasm. Tissue specificity: Ubiquitous. Also known as: Superoxide dismutase copper chaperone, CCS, Copper chaperone for superoxide dismutase, Superoxide Dismutase 4.

Specificity: Appears to be specific for CCS.

Application Details

Application Notes: IHC, WB. A dilution of 1: 300 to 1: 2000 is recommended. The optimal dilution should be determined by the end user. Not yet tested in other applications.

Purity: whole serum

Storage: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Restrictions: For Research Use only

Publications

Culotta, Klomp, Strain et al.: "The copper chaperone for superoxide dismutase." in: The Journal of biological chemistry, Vol. 272, Issue 38, pp. 23469-72, 1997 (PubMed).

Casareno, Waggoner, Gitlin: "The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase." in: The Journal of biological chemistry, Vol. 273, Issue 37, pp. 23625-8, 1998 (PubMed).

Lamb, Wernimont, Pufahl et al.: "Crystal structure of the second domain of the human copper chaperone for superoxide dismutase." in: Biochemistry, Vol. 39, Issue 7, pp. 1589-95, 2000 (PubMed).

Stasser, Eisses, Barry et al.: "Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface." in: Biochemistry, Vol. 44, Issue 9, pp. 3143-52, 2005 (PubMed).

Molina, Horn, Tang et al.: "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, Issue 7, pp. 2199-204, 2007 (PubMed).