Superoxide Dismutase4 (SOD4) (Internal Region) antibody

Details for Product No. ABIN350845
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Antigen
Synonyms SODCC.2, sod4ap
Epitope
Internal Region
(1), (1)
Reactivity
Human, Mouse (Murine)
(16), (15), (13), (12), (12), (12)
Host
Rabbit
(17), (2)
Clonality
Polyclonal
Conjugate
Un-conjugated
(1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Immunohistochemistry (IHC), Western Blotting (WB)
(10), (9), (8), (6), (4), (4), (2), (1)
Pubmed 5 references available
Quantity 100 μL
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Catalog No. ABIN350845
454.67 $
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Immunogen A synthetic peptide from the internal region of human SOD4 (CCS, Copper chaperone for superoxide dismutase, Superoxide Dismutase 4) conjugated to an immunogenic carrier protein was used as the antigen. The antigen shares 95% and 92% identity with mouse and rat sequence respectively.
Specificity Specific for CCS.
Purification Whole serum
Alternative Name SOD4
Background 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.
Application Notes 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.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment 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.
Expiry Date 12 months
General 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).

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