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AB196433

Recombinant Human Metnase protein (DDDDK tag N-Terminus)

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Recombinant Human Metnase protein (DDDDK tag N-Terminus) is a Human Fragment protein, in the 27 to 684 aa range, expressed in Mammalian, with >30%, suitable for SDS-PAGE, FuncS.

View Alternative Names

Histone-lysine N-methyltransferase SETMAR, SET domain and mariner transposase fusion protein, Metnase, SETMAR

2 Images
SDS-PAGE - Recombinant Human Metnase protein (DDDDK tag N-Terminus) (AB196433)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Metnase protein (DDDDK tag N-Terminus) (AB196433)

SDS-PAGE analysis of 3 μg of ab196433 on 10% SDS-PAGE gel stained with Coomassie.

SDS-PAGE - Recombinant Human Metnase protein (DDDDK tag N-Terminus) (AB196433)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Metnase protein (DDDDK tag N-Terminus) (AB196433)

SDS-PAGE analysis of 2 μg of ab196433 on 10% SDS-PAGE gel stained with Coomassie.

Key facts

Purity

>30% SDS-PAGE

Expression system

Mammalian

Tags

DDDDK tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

No

Accession

Q53H47

Animal free

No

Carrier free

No

Species

Human

Storage buffer

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

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

The protein fragment was expressed in FreeStyle 293-F cells.

Previously labelled as SETMAR.

Sequence info

[{"sequence":"QLDVACGQENLPVGAWPPGAAPAPFQYTPDHVVGPGADIDPTQITFPGCICVKTPCLPGTCSCLRHGENYDDNSCLRDIGSGGKYAEPVFECNVLCRCSDHCRNRVVQKGLQFHFQVFKTHKKGWGLRTLEFIPKGRFVCEYAGEVLGFSEVQRRIHLQTKSDSNYIIAIREHVYNGQVMETFVDPTYIGNIGRFLNHSCEPNLLMIPVRIDSMVPKLALFAAKDIVPEEELSYDYSGRYLNLTVSEDKERLDHGKLRKPCYCGAKSCTAFLPFDSSLYCPVEKSNISCGNEKEPSMCGSAPSVFPSCKRLTLETMKMMLDKKQIRAIFLFEFKMGRKAAETTRNINNAFGPGTANERTVQWWFKKFCKGDESLEDEERSGRPSEVDNDQLRAIIEADPLTTTREVAEELNVNHSTVVRHLKQIGKVKKLDKWVPHELTENQKNRRFEVSSSLILRNHNEPFLDRIVTCDEKWILYDNRRRSAQWLDQEEAPKHFPKPILHPKKVMVTIWWSAAGLIHYSFLNPGETITSEKYAQEIDEMNQKLQRLQLALVNRKGPILLHDNARPHVAQPTLQKLNELGYEVLPHPPYSPDLLPTNYHVFKHLNNFLQGKRFHNQQDAENAFQEFVESQSTDFYATGINQLISRWQKCVDCNGSYFD","proteinLength":"Fragment","predictedMolecularWeight":"76 kDa","actualMolecularWeight":null,"aminoAcidEnd":684,"aminoAcidStart":27,"nature":"Recombinant","expressionSystem":"Mammalian","accessionNumber":"Q53H47","tags":[{"tag":"DDDDK","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False

Specifications

Form

Liquid

General info

Function

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).

Sequence similarities

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

Product protocols

Target data

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).
See full target information SETMAR

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