SETMAR Antibody
(Synonyms: Histone-lysine N-methyltransferase SETMAR, SET domain and mariner transposase fusion protein, Metnase, SETMAR)SETMAR Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to SETMAR.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 | 1:50-200 |
Product Details
SETMAR Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to SETMAR.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 41 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 78 kDa
Synthetic peptide corresponding to the center region of human SETMAR.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
SETMAR is a 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. 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. Also regulates replication fork processing, promoting replication fork restart and regulating DNA decatenation through stimulation of the topoisomerase activity of TOP2A[1][2][3][4][5][6][7][8][9][10][11].
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Subcellular Localization
Nucleus; Chromosome
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Expression
Tissue_Specificity: Widely expressed, with highest expression in placenta and ovary and lowest expression in skeletal muscle. -
Isoforms & Post-Translational Modification
SETMAR has 3 isoforms, Q53H47-1: amino acid length is 684, molecular weight is 78034 Da (predicted); Q53H47-2: amino acid length is 365, molecular weight is 40510 Da (predicted); Q53H47-3: amino acid length is 545, molecular weight is 62124 Da (predicted).Methylated. Methylation regulates activity in DNA decatenation
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Subunit
Homodimer.
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SwissProt ID
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Synonyms
Histone-lysine N-methyltransferase SETMAR, SET domain and mariner transposase fusion protein, Metnase, SETMAR
Documentation
References
[1]. Lee SH, et al. The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair. Proc Natl Acad Sci U S A. 2005 Dec 13;102(50):18075-80. [Content Brief]
[2]. Cordaux R, et al. Birth of a chimeric primate gene by capture of the transposase gene from a mobile element. Proc Natl Acad Sci U S A. 2006 May 23;103(21):8101-6. [Content Brief]
[3]. Miskey C, et al. The ancient mariner sails again: transposition of the human Hsmar1 element by a reconstructed transposase and activities of the SETMAR protein on transposon ends. Mol Cell Biol. 2007 Jun;27(12):4589-600. [Content Brief]
[4]. Roman Y, et al. Biochemical characterization of a SET and transposase fusion protein, Metnase: its DNA binding and DNA cleavage activity. Biochemistry. 2007 Oct 9;46(40):11369-76. [Content Brief]
[5]. Beck BD, et al. Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair. J Biol Chem. 2008 Apr 4;283(14):9023-30. [Content Brief]
[6]. Goodwin KD, et al. Crystal structure of the human Hsmar1-derived transposase domain in the DNA repair enzyme Metnase. Biochemistry. 2010 Jul 13;49(27):5705-13. [Content Brief]
[7]. Hromas R, et al. Chk1 phosphorylation of Metnase enhances DNA repair but inhibits replication fork restart. Oncogene. 2012 Sep 20;31(38):4245-54. [Content Brief]
[8]. Kim HS, et al. The DDN catalytic motif is required for Metnase functions in non-homologous end joining (NHEJ) repair and replication restart. J Biol Chem. 2014 Apr 11;289(15):10930-10938. [Content Brief]
[9]. Fnu S, et al. Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. Proc Natl Acad Sci U S A. 2011 Jan 11;108(2):540-5. [Content Brief]
[10]. Williamson EA, et al. The SET and transposase domain protein Metnase enhances chromosome decatenation: regulation by automethylation. Nucleic Acids Res. 2008 Oct;36(18):5822-31. [Content Brief]
[11]. De Haro LP, et al. Metnase promotes restart and repair of stalled and collapsed replication forks. Nucleic Acids Res. 2010 Sep;38(17):5681-91. [Content Brief]
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