anti-sodC antibody product blog
Tags: Antibody; Polyclonal Antibody; Superoxide Dismutase, Cu,Zn; anti-sodC antibody; sodC;
The sodC sodc (Catalog #MBS621989) is an Antibody produced from Rabbit and is intended for research purposes only. The product is available for immediate purchase. The Superoxide Dismutase, Cu,Zn (SOD Cu,Zn) reacts with Mouse, Rat and may cross-react with other species as described in the data sheet. MyBioSource\'s Superoxide Dismutase, Cu,Zn can be used in a range of immunoassay formats including, but not limited to, ELISA (EL/EIA), Western Blot (WB).Dilution: Western Blot (ECL): 1ug/ml
Optimal dilutions to be determined by researcher.
Note:
This antibody is recommended for use with samples of mouse or rat origin.
Positive Controls:
Rat Brain Tissue Extract and Mouse Brain Tissue Extract. Researchers should empirically determine the suitability of the sodC sodc for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.
The sodC sodc product has the following accession number(s) (GI #16129604) (NCBI Accession #NP_416163.1) (Uniprot Accession #P0AGD1). Researchers may be interested in using Bioinformatics databases such as those available at The National Center for Biotechnology Information (NCBI) website for more information about accession numbers and the proteins they represent. Even researchers unfamiliar with bioinformatics databases will find the NCBI databases to be quite user friendly and useful.
To buy or view more detailed product information and pricing, please click on the technical datasheet page below:
Please refer to the product datasheet for known applications of a given antibody. We\'ve tested the Superoxide Dismutase, Cu,Zn (SOD Cu,Zn) with the following immunoassay(s):
Western Blot (WB) (Western blot analysis: rat brain tissue extract, probed with MBS621989)
Cu/Zn containing superoxide dismutase (SOD) belongs to the family of related enzymes which have the same catalytic function but are structurally different. SOD catalyzes the dismutation of the superoxide radical O2-to O2 and H2O2 which in turn is metabolized to H2O and O2 by catalase and glutathione peroxidase (1, 2). The SOD family is classified into subfamilies on the basis of their metal cofactors which could be either a dinuclear Cu/Zn or mononuclear Fe, Mn or Ni. The Fe-and Mn-SODs have identical metal chelating residues at the active site and share substantial sequence and tertiary homology, whereas the other SODs are structurally unrelated. The Cu/Zn-SOD is found in the cytosol of eukaryotes, in chloroplasts and in the periplasm of some prokaryotes. The eukaryotic, Cu/Zn-SODs usually consists of two identical subunits of 16kD each that are linked by two cysteines forming an intrasubunit disulfide bridge and each subunit contains a metal cluster at the active site. The Cu/Zn-SOD is believed to play a major role in antioxidant defence mechanisms (3,5). Fe-SOD is present in both aerobic and anaerobic bacteria, Archaea and plants whereas Mn-SOD is present in bacteria, Archaea, mitochondria and chloroplasts. In animals, Mn-SOD is present predominately in the mitochondria as a tetramer of 80kD (3,4). SODs are involved in maintaining the cell integrity and protecting the functionality of the single cell components against the damages by oxidative stress (5).