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Superoxide Dismutase4 (SOD4) (Internal Region) antibody

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Synonyms SODCC.2, sod4ap
Internal Region
(1), (1), (1), (1)
Human, Mouse (Murine)
(10), (3), (2)
(7), (7)
Immunohistochemistry (IHC), Western Blotting (WB)
(13), (11), (6), (6), (6), (5), (3)
Pubmed 5 references available
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Quantity 500 μg
Shipping to United States ( )
Availability Will be delivered in 7 to 8 Business Days
Immunogen A synthetic peptide from the internal region of human SOD4 conjugated to blue carrier protein was used as the antigen. The peptide shares 95% and 92% identity with mouse and rat sequence respectively.
Isotype IgG
Specificity Specific for CCS.
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 concentration of 10-50 µg/ml is recommended.
The optimal concentration should be determined by the end user.
Not yet tested in other applications.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 500 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
Background publications 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).

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).

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).

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).

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).

Catalog No. ABIN350846
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