SOD1

GWB-F69CF5

A synthetic peptide corresponding to residues near the N-terminus of human SOD1 was used as an immunogen.

WB: 1:1 000-2 000IHC: 1:250-500ICC: 1:50-100FC: 1:80IP: 1:50. The eukaryotic copper zinc superoxide dismutases are remarkably stable dimeric proteins that maintain an intrasubunit disulfide bond in the reducing environment of the cytosol and are active under a variety of stringent denaturing conditions. The structural interplay of conserved disulfide bond and metal-site occupancy in human copper zinc superoxide dismutase (SOD1) is of increasing interest as these post-translational modifications are known to dramatically alter the catalytic chemistry the subcellular localization and the susceptibility of the protein to aggregation (1). Defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). A crystal structure of human SOD along with two other SOD structures established that all 12 observed FALS mutant sites alter conserved interactions critical to the beta-barrel fold and dimer contact rather than catalysis (2). 1. Xiao L Wang YC Li WS et al The role of mTOR and phospho-p70S6K in pathogenesis and progression of gastric carcinomas: an immunohistochemical study on tissue microarray J Exp Clin Cancer Res 28 (2009) : 152[Application: IHC]1. Hay N. ; Sonenberg N. :Genes Dev. 18: 1926-1945 2004. 2. Manufactured under U. S. Patents No. 5 675 063 and 7 429 487