MutM (AA 1-269) protein (His tag)
Origin: E. coli
Host: Escherichia coli (E. coli)
Recombinant
> 90% by SDS-PAGE
SDS
1 image
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- Target
- MutM
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-269
- Origin
- E. coli
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- His tag
- Application
- SDS-PAGE (SDS)
- Sequence
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MPELPEVETS RRGIEPHLVG ATILHAVVRN GRLRWPVSEE IYRLSDQPVL SVQRRAKYLL LELPEGWIII HLGMSGSLRI LPEELPPEKH DHVDLVMSNG KVLRYTDPRR FGAWLWTKEL EGHNVLTHLG PEPLSDDFNG EYLHQKCAKK KTAIKPWLMD NKLVVGVGNI YASESLFAAG IHPDRLASSL SLAECELLAR VIKAVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK GEPCRVCGTP IVATKHAQRA TFYCRQCQK - Purification
- purified by chromatography
- Purity
- > 90% by SDS-PAGE
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.5 mg/mL
- Buffer
- 20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol 0.1 M NaCl,1 MM DTT
- Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Can be stored at +2°C to +8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C. Avoid repeated freezing and thawing cycles.
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- Target
- MutM
- Background
- 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.
- Molecular Weight
- 32.4 kDa (289aa) confirmed by MALDI-TOF
- NCBI Accession
- NP_418092
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