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Cell-permeable superoxide dismutase (SOD) mimetic. Catalyzes the dismutation of O2– • (rate constant ~4 x 107 M-1 s-1) even in the presence of excess EDTA. Can substitute for SOD in mutants of E. coli lacking this enzyme. MnTMPyP acts in vivo as an NADPH/GSH:O2• oxidoreductase rather than as an SOD mimetic. Also an efficient peroxynitrite reductase when redox-coupled with biological antioxidants.
Izbicka, E., et al. 1999. Cancer Res.59, 639. Lee, J., et al. 1998. J. Am. Chem. Soc. 120, 6053. Gardner, P.R., et al. 1996. Arch. Biochem. Biophys. 325, 20. Liochev, S.I., and Fridovich, I. 1995. Arch. Biochem. Biophys. 321, 271. Faulkner, K.M., et al. 1994. J. Biol. Chem. 269, 23471.
Izbicka, E., et al. 1999. Cancer Res.59, 639. Lee, J., et al. 1998. J. Am. Chem. Soc. 120, 6053. Gardner, P.R., et al. 1996. Arch. Biochem. Biophys. 325, 20. Liochev, S.I., and Fridovich, I. 1995. Arch. Biochem. Biophys. 321, 271. Faulkner, K.M., et al. 1994. J. Biol. Chem. 269, 23471.
Anthony R. White, et al. (2006) Degradation of the alzheimer disease amyloid -peptide by metal-dependent up-regulation of metalloprotease activity. journal of Biological Chemistry281, 17670-17680.
数据表
Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.
Cell-permeable superoxide dismutase (SOD) mimetic. Catalyzes the dismutation of O2– • (rate constant ~4 x 107 M-1 s-1) even in the presence of excess EDTA. Can substitute for SOD in mutants of E. coli lacking this enzyme. MnTMPyP acts in vivo as an NADPH/GSH:O2• oxidoreductase rather than as an SOD mimetic. Also an efficient peroxynitrite reductase when redox-coupled with biological antioxidants.
Form
Black solid
Chemical formula
C₇₂H₆₅MnN₈O₁₃S₄
Structure formula
Purity
≥95% by TLC
Solubility
H₂O (1 mg/ml)
Storage
Protect from moisture
Protect from light
-20°C
Do Not Freeze
Ok to freeze
Special Instructions
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Toxicity
Standard Handling
References
Izbicka, E., et al. 1999. Cancer Res.59, 639. Lee, J., et al. 1998. J. Am. Chem. Soc. 120, 6053. Gardner, P.R., et al. 1996. Arch. Biochem. Biophys. 325, 20. Liochev, S.I., and Fridovich, I. 1995. Arch. Biochem. Biophys. 321, 271. Faulkner, K.M., et al. 1994. J. Biol. Chem. 269, 23471.
Citation
Anthony R. White, et al. (2006) Degradation of the alzheimer disease amyloid -peptide by metal-dependent up-regulation of metalloprotease activity. journal of Biological Chemistry281, 17670-17680.
