protein

Recombinant Mouse Superoxide dismutase [Cu-Zn]

MBS962699

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Mouse Superoxide dismutase [Cu-Zn]

Superoxide dismutase [Cu-Zn]

superoxide dismutase; Superoxide dismutase [Cu-Zn]; superoxide dismutase [Cu-Zn]; superoxide dismutase 1, soluble

Sod1

Sod1; Sod1; Ipo1; SODC; Ipo-1; Sod-1; CuZnSOD; Cu/Zn-SOD; B430204E11Rik

SODC_MOUSE

E Coli or Yeast or Baculovirus or Mammalian Cell

2-154

154

AMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLT
EGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEE
RHVGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTM
VVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

cDNA and deduced amino acid sequence of murine Cu-Zn superoxide dismutase.Bewley G.C.Nucleic Acids Res. 16:2728-2728(1988) Isolation and analysis of the mouse genomic sequence encoding Cu(2+) -Zn2+ superoxide dismutase.Benedetto M.T., Anzai Y., Gordon J.W.Gene 99:191-195(1991) Purification of an inhibitor of erythroid progenitor cell cycling and antagonist to interleukin 3 from mouse marrow cell supernatants and its identification as cytosolic superoxide dismutase.Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S., Hulmes J.D., Blum M., Axelrad A.A.J. Cell Biol. 111:1217-1223(1990) Lubec G., Klug S., Sunyer B., Chen W.-Q.Submitted (JAN-2009) to UniProtKB Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein.Wang S.K., Weaver J.D., Zhang S., Lei X.G.Free Radic. Biol. Med. 51:197-204(2011) SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.Mol. Cell 50:919-930(2013) Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) Structures of mouse SOD1 and human/mouse SOD1 chimeras.Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J.Arch. Biochem. Biophys. 503:183-190(2010)

45597447

NP_035564.1

NM_011434.1

P08228

19.9kD

Amyotrophic Lateral Sclerosis (ALS) Pathway (83296); Amyotrophic Lateral Sclerosis (ALS) Pathway (511); Cellular Responses To Stress Pathway (1324506); Detoxification Of Reactive Oxygen Species Pathway (1324512); Hemostasis Pathway (1323559); Huntington's Disease Pathway (83297); Huntington's Disease Pathway (512); Longevity Regulating Pathway - Multiple Species (1340727); Longevity Regulating Pathway - Multiple Species (1340651); One Carbon Metabolism And Related Pathways (198380)

SOD1: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Homodimer; non-disulfide linked. Homodimerization may take place via the ditryptophan cross-link at Trp-33. The pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 interact with RNF19A, whereas wild-type protein does not. The pathogenic variants ALS1 Arg-86 and Ala-94 interact with MARCH5, whereas wild-type protein does not. Belongs to the Cu-Zn superoxide dismutase family. Protein type: EC 1.15.1.1; Apoptosis; Nuclear receptor co-regulator; Oxidoreductase; Mitochondrial. Cellular Component: cell soma; cytoplasm; cytoplasmic vesicle; cytosol; dendrite cytoplasm; extracellular matrix; extracellular region; extracellular space; lysosome; mitochondrial intermembrane space; mitochondrion; myelin sheath; neuron projection; nucleoplasm; nucleus; peroxisome; plasma membrane; protein complex; secretory granule. Molecular Function: antioxidant activity; chaperone binding; copper ion binding; enzyme binding; identical protein binding; metal ion binding; oxidoreductase activity; protein binding; protein phosphatase 2B binding; Rac GTPase binding; superoxide dismutase activity; zinc ion binding. Biological Process: activation of MAPK activity; aging; anterograde axon cargo transport; auditory receptor cell stereocilium organization and biogenesis; cell aging; cellular iron ion homeostasis; embryo implantation; glutathione metabolic process; heart contraction; hydrogen peroxide biosynthetic process; locomotory behavior; muscle maintenance; myelin maintenance in the peripheral nervous system; myeloid cell homeostasis; negative regulation of apoptosis; negative regulation of cholesterol biosynthetic process; negative regulation of neuron apoptosis; neurofilament cytoskeleton organization and biogenesis; ovarian follicle development; positive regulation of catalytic activity; positive regulation of cytokine production; positive regulation of superoxide release; regulation of blood pressure; regulation of GTPase activity; regulation of mitochondrial membrane potential; regulation of multicellular organism growth; regulation of protein kinase activity; relaxation of vascular smooth muscle; removal of superoxide radicals; response to axon injury; response to copper ion; response to drug; response to ethanol; response to heat; response to hydrogen peroxide; response to nutrient levels; response to organic substance; response to oxidative stress; response to reactive oxygen species; response to superoxide; retinal homeostasis; retrograde axon cargo transport; sensory perception of sound; spermatogenesis; superoxide metabolic process; superoxide release; transmission of nerve impulse

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750