Anti-Superoxide Dismutase 3/SOD3 Antibody Picoband® 0,00647 Vervoeging

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 though 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.

Extracellular superoxide dismutase [Cu-Zn]; EC-SOD;1.15.1.1; SOD3

SOD3

6649

P08294

Human

No cross-reactivity with other proteins

A synthetic peptide corresponding to a sequence at the N-terminus of human SOD3.

Expressed in blood vessels, heart, lung, kidney and placenta. Major SOD isoenzyme in extracellular fluids such as plasma, lymph and synovial fluid.

Flow Cytometry

Cancer, Cancer Metabolism, Cell Biology, Metabolism, Metabolism Processes, Oxidative Stress, Pathways and Processes, Redox Metabolism, Response To Hypoxia

Immunogen affinity purified.

Liquid

Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.

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.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

25851 MW

No cross reactivity with other proteins.

6

Extracellular superoxide dismutase [Cu-Zn]

Secreted, extracellular space. 99% of EC-SOD is anchored to heparan sulfate proteoglycans in the tissue interstitium, and 1% is located in the vasculature in equilibrium between the plasma and the endothelium.

Belongs to the Cu-Zn superoxide dismutase family.

Extracellular superoxide dismutase[Cu-Zn]

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.