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Products Polyclonal Anti-SOD3
| Catalogue number: | PA1899 |
| Price: | $200.00 |
| Reactivities: | Human |
| Applications: | Immunocytochemistry, Immunohistochemistry, Immunohistochemistry - frozen, Western Blot |
| Size: | 100ug/vial |
| Gene: | SOD3 |
| Swiss prot: | P08294 |
| Form: | Lyophilized |
| Format: | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. |
| Storage temp: | At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.Avoid repeated freezing and thawing. |
| Scientific background: | SOD3(SUPEROXIDE DISMUTASE 3) also called SUPEROXIDE DISMUTASE, EXTRACELLULAR, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM. |
| References: | 1. Folz, R. J., Crapo, J. D.Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene.Genomics 22: 162-171, 1994. 2. Hjalmarsson, K., Marklund, S. L., Engstrom, A., Edlund, T.Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase.Proc. Nat. Acad. Sci. 84: 6340-6344, 1987. 3. Stern, L.F., Chapman, N. H., Wijsman, E. M., Altherr, M. R., Rosen, D. R.Assignment of SOD3 to human chromosome band 4p15.3-p15.1 with somatic cell and radiation hybrid mapping, linkage mapping, and fluorescent in-situ hybridization.Cytogenet. Genome Res. 101: 178 only, 2003. |
| Additional info: | A synthetic peptide corresponding to a sequence at the N-terminal of human SOD3. |
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