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

Produktnummer ABIN1098227

Dieses Recombinant -Protein wird in Escherichia coli (E. coli) produziert.

Kurzübersicht für MutM (AA 1-269) protein (His tag) (ABIN1098227)

Target: MutM

Protein-Typ: Recombinant

Spezies: E. coli

Quelle: Escherichia coli (E. coli)

Applikation: SDS-PAGE (SDS)

Reinheit: > 90% by SDS-PAGE

Produktdetails

Proteineigenschaft: AA 1-269

Aufreinigungstag / Konjugat: His tag

Sequenz: 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

Aufreinigung: purified by chromatography

Anwendungsinformationen

Applikationshinweise: Optimal working dilution should be determined by the investigator.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Konzentration: 0.5 mg/mL

Buffer: 20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol 0.1 M NaCl,1 MM DTT

Lagerung: 4 °C,-20 °C,-80 °C

Informationen zur Lagerung: 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.

Antigendetails

Target: MutM

Hintergrund: 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.

Molekulargewicht: 32.4 kDa (289aa) confirmed by MALDI-TOF

NCBI Accession: NP_418092