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MutM (AA 1-269) protein (His tag)

This Recombinant protein is produced in Escherichia coli (E. coli).
Catalog No. ABIN1098227

Quick Overview for MutM (AA 1-269) protein (His tag) (ABIN1098227)

Target

MutM

Protein Type

Recombinant

Origin

E. coli

Source

  • 1
Escherichia coli (E. coli)

Application

SDS-PAGE (SDS)

Purity

> 90% by SDS-PAGE
  • Protein Characteristics

    AA 1-269

    Purification tag / Conjugate

    His tag

    Sequence

    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
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  • Application Notes

    Optimal working dilution should be determined by the investigator.

    Restrictions

    For Research Use only
  • 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.
  • 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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