Recombinant Human Metnase protein (GST tag N-Terminus)
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- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Metnase protein (GST tag N-Terminus) (AB125543)
SDS-PAGE analysis of ab125543.
Reactivity 정보
제품 세부 정보
서열 정보
특성 및 보관 정보
제형
Purification 테크닉
배송 시 보관 조건
적절한 단기 보관 조건
적절한 장기 보관 조건
분주 정보
보관 정보
일반 정보
기능
Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double-strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Also has kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity (PubMed : 16332963, PubMed : 16672366, PubMed : 17403897, PubMed : 17877369, PubMed : 18263876, PubMed : 20521842, PubMed : 22231448, PubMed : 24573677). In parallel, has a histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of histone H3. Specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining (PubMed : 16332963, PubMed : 21187428, PubMed : 22231448). Also regulates replication fork processing, promoting replication fork restart and regulating DNA decatenation through stimulation of the topoisomerase activity of TOP2A (PubMed : 18790802, PubMed : 20457750).
서열 유사성
In the N-terminal section; belongs to the class V-like SAM-binding methyltransferase superfamily.. In the C-terminal section; belongs to the mariner transposase family.
Post-translational modifications
Methylated. Methylation regulates activity in DNA decatenation.. Phosphorylated at Ser-508 by CHEK1 and dephosphorylated by protein phosphatase 2A/PP2A. Phosphorylation at Ser-508 is enhanced by DNA damage and promotes recruitment to damaged DNA. It stimulates DNA repair and impairs replication fork restart.
Subcellular localisation
Nucleus
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