Recombinant Human Metnase protein is a Human Fragment protein, in the 27 to 684 aa range, expressed in Mammalian, with >=30% purity and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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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. Has also 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).
Histone-lysine N-methyltransferase SETMAR, SET domain and mariner transposase fusion protein, Metnase, SETMAR
Recombinant Human Metnase protein is a Human Fragment protein, in the 27 to 684 aa range, expressed in Mammalian, with >=30% purity and suitable for SDS-PAGE, FuncS.
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.72% Sodium chloride, 0.63% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride
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. Has also 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).
In the N-terminal section; belongs to the class V-like SAM-binding methyltransferase superfamily.
Methylated. Methylation regulates activity in DNA decatenation.
The protein fragment was expressed in FreeStyle 293-F cells.
Previously labelled as SETMAR.
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SDS-PAGE analysis of 2 μg of ab196433 on 10% SDS-PAGE gel stained with Coomassie.
SDS-PAGE analysis of 3 μg of ab196433 on 10% SDS-PAGE gel stained with Coomassie.
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