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Anti-Superoxide Dismutase 3/SOD3 Antibody Picoband® Fluoro647 Conjugated

Product Specifications

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.

Synonyms

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

Gene Name

SOD3

Gene ID

6649

UniProt

P08294

Host

Rabbit

Reactivity

Human

Cross Reactivity

No cross-reactivity with other proteins.

Immunogen

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

Clonality

Polyclonal

Tissue Specificity

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

Applications

Flow Cytometry

Field of Research

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

Purification

Immunogen affinity purified.

Form

Liquid

Function

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

References & Citations

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.

Storage Conditions

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

Product Datasheet

https://www.bosterbio.com/datasheet?sku=A01784-1-Fluoro647

Calculated Molecular Weight

57862 MW

Specificity

No cross reactivity with other proteins.

Applications Notes

6

Gene Name Synonym

Superoxide dismutase 3, extracellular

Subcellular Location

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.

Isotype

Rabbit IgG

Contents

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

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