Recombinant e.coli mutM protein
€0.00
In stock
SKU
ATGP1448
Description
mutM, also known as formamidopyrimidine DNA glycosylase, is a base excision repair enzyme which recognizes and removes a wide range of oxidized purines from correspondingly damaged DNA. This protein is nonredundant and required to rapidly remove its substrate lesions on the chromosome. In addition, it also repaired a significant portion of the lesions recognized by Endo III, suggesting that it plays a prominent role in the global repair of both purine damage and pyrimidine damage in vivo. Recombinant E. coli mutM protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.Alternative Names
Formamidopyrimidine-DNA glycosylase, fpgConcentration
0.5mg/ml (determined by Bradford assay)Concentration
Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 20% glycerol 0.1M NaCl,1mM DTTStorage: Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
mutM, also known as formamidopyrimidine DNA glycosylase, is a base excision repair enzyme which recognizes and removes a wide range of oxidized purines from correspondingly damaged DNA. This protein is nonredundant and required to rapidly remove its substrate lesions on the chromosome. In addition, it also repaired a significant portion of the lesions recognized by Endo III, suggesting that it plays a prominent role in the global repair of both purine damage and pyrimidine damage in vivo. Recombinant E. coli mutM protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.Alternative Names
Formamidopyrimidine-DNA glycosylase, fpgConcentration
0.5mg/ml (determined by Bradford assay)Concentration
Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 20% glycerol 0.1M NaCl,1mM DTTStorage: Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
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