XRCC4 Antibody (YA1082)(PBS only)
(Synonyms: X ray repair cross complementing protein 4; DNA repair protein XRCC4; DNA double strand break repair)XRCC4 Antibody (YA1082) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to XRCC4.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, IHC-F, IHC-P, ICC/IF, IP
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS, pH 7.4.
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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 |
IP
IP: Immunoprecipitation
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|---|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 50-1:100 | 1:50-1:200 | 1:20 |
Product Details
XRCC4 Antibody (YA1082) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to XRCC4.
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Host Mouse
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 38-45 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: 38 kDa
Synthetic Peptide of XRCC4
Affinity Purified
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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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
XRCC4 is a DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination. Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs). Associates with NHEJ1/XLF to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired. The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other. The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors. Plays a key role in the NHEJ ligation step of the broken DNA during DSB repair via direct interaction with DNA ligase IV (LIG4): the LIG4-XRCC4 subcomplex reseals the DNA breaks after the gap filling is completed. XRCC4 stabilizes LIG4, regulates its subcellular localization and enhances LIG4's joining activity. Binding of the LIG4-XRCC4 subcomplex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. Promotes displacement of PNKP from processed strand break termini; Acts as an activator of the phospholipid scramblase activity of XKR4. This form, which is generated upon caspase-3 (CASP3) cleavage, translocates into the cytoplasm and interacts with XKR4, thereby promoting phosphatidylserine scramblase activity of XKR4 and leading to phosphatidylserine exposure on apoptotic cell surface[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25].
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Subcellular Localization
Nucleus; Chromosome; Cytoplasm
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Expression
Tissue_specificity:Broad expression -
Isoforms & Post-Translational Modification
Q13426 has 3 isomers: Q13426-1: 38287 Da (predicted); Q13426-2: 38058 Da (predicted); Q13426-3: 35372 Da (predicted).
Phosphorylated by PRKDC at the C-terminus in response to DNA damage; Ser-260 and Ser-320 constitute the main phosphorylation sites (PubMed:12547193, PubMed:14599745, PubMed:15177042, PubMed:26666690, PubMed:28500754, PubMed:30247612, PubMed:9430729). Phosphorylations by PRKDC at the C-terminus of XRCC4 and NHEJ1/XLF are highly redundant and regulate ability of the XRCC4-NHEJ1/XLF subcomplex to bridge DNA (PubMed:22228831, PubMed:28500754). Phosphorylation by PRKDC does not prevent interaction with NHEJ1/XLF but disrupts ability to bridge DNA and promotes detachment from DNA (PubMed:22228831, PubMed:28500754). Phosphorylation at Ser-327 and Ser-328 by PRKDC promotes recognition by the SCF(FBXW7) complex and subsequent ubiquitination via 'Lys-63'-linked ubiquitin (PubMed:26774286). Phosphorylation at Thr-233 by CK2 promotes interaction with PNKP; regulating PNKP activity and localization to DNA damage sites (PubMed:15385968, PubMed:20852255, PubMed:28453785). Phosphorylation by CK2 promotes interaction with APTX (PubMed:15380105);Ubiquitinated at Lys-296 by the SCF(FBXW7) complex via 'Lys-63'-linked ubiquitination, thereby promoting double-strand break repair: the SCF(FBXW7) complex specifically recognizes XRCC4 when phosphorylated at Ser-327 and Ser-328 by PRKDC, and 'Lys-63'-linked ubiquitination facilitates DNA non-homologous end joining (NHEJ) by enhancing association with XRCC5/Ku80 and XRCC6/Ku70 (PubMed:26774286). Monoubiquitinated (PubMed:16412978);Undergoes proteolytic processing by caspase-3 (CASP3) (Probable) (PubMed:33725486). This generates the protein XRCC4, C-terminus (XRCC4/C), which translocates to the cytoplasm and activates phospholipid scramblase activity of XKR4, thereby promoting phosphatidylserine exposure on apoptotic cell surface (PubMed:33725486) -
Subunit
Homodimer and homotetramer in solution (PubMed:11080143, PubMed:25574025, PubMed:25670504, PubMed:25941166, PubMed:31548606, PubMed:17567543). Interacts with NHEJ1/XLF; the interaction is direct and is mediated via a head-to-head interaction between N-terminal head regions (PubMed:16439205, PubMed:17567543, PubMed:18158905, PubMed:20558749, PubMed:21768349, PubMed:21775435, PubMed:21936820, PubMed:22228831, PubMed:22287571, PubMed:22658747, PubMed:26100018, PubMed:27437582). Interacts with LIG4; the LIG4-XRCC4 subcomplex has a 1:2 stoichiometry and XRCC4 is required for LIG4 stability (PubMed:11702069, PubMed:12517771, PubMed:17290226, PubMed:19332554, PubMed:21982441, PubMed:22658747, PubMed:24984242, PubMed:25934149, PubMed:9242410, PubMed:9259561, PubMed:17567543). Component of the core long-range non-homologous end joining (NHEJ) complex (also named DNA-PK complex) composed of PRKDC, LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (PubMed:10757784, PubMed:10854421, PubMed:12547193, PubMed:17124166, PubMed:22658747, PubMed:26774286, PubMed:33854234, PubMed:34352203). Additional component of the NHEJ complex includes PAXX (PubMed:16439205). Following autophosphorylation, PRKDC dissociates from DNA, leading to formation of the short-range NHEJ complex, composed of LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (PubMed:33854234). Interacts with PRKDC; the interaction is direct (PubMed:12509254). Interacts with XRCC6/Ku70; the interaction is direct (PubMed:17124166). Interacts with APTX and APLF (PubMed:15380105, PubMed:17353262, PubMed:17396150, PubMed:18077224). Forms a heterotetramer with IFFO1; the interaction involves LIG4-free XRCC4 and leads to the relocalization of IFFO1 to the sites of DNA damage (PubMed:31548606). Interacts with PNKP; mainly interacts with PNKP when phosphorylated at Thr-233, but is also able to interact at much lower level with PNKP when not unphosphorylated (PubMed:15385968, PubMed:20852255, PubMed:28453785). Interacts with POLL (DNA polymerase lambda) (PubMed:30250067)
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SwissProt ID
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Synonyms
X ray repair cross complementing protein 4; DNA repair protein XRCC4; DNA double strand break repair
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Research Field
Epigenetics and Nuclear Signaling
Documentation
References
[1]. Nick McElhinny SA, et al. Ku recruits the XRCC4-ligase IV complex to DNA ends. Mol Cell Biol. 2000 May;20(9):2996-3003. [Content Brief]
[2]. Chen L, et al. Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase. J Biol Chem. 2000 Aug 25;275(34):26196-205. [Content Brief]
[3]. Lee JW, et al. Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro. Cancer Res. 2003 Jan 1;63(1):22-4. [Content Brief]
[4]. Foster RE, et al. Monoubiquitination of the nonhomologous end joining protein XRCC4. Biochem Biophys Res Commun. 2006 Mar 3;341(1):175-83. [Content Brief]
[5]. Mari PO, et al. Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4. Proc Natl Acad Sci U S A. 2006 Dec 5;103(49):18597-602. [Content Brief]
[6]. Gu J, et al. XRCC4:DNA ligase IV can ligate incompatible DNA ends and can ligate across gaps. EMBO J. 2007 Feb 21;26(4):1010-23. [Content Brief]
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[8]. Wanotayan R, et al. Asparagine 326 in the extremely C-terminal region of XRCC4 is essential for the cell survival after irradiation. Biochem Biophys Res Commun. 2015 Feb 20;457(4):526-31. [Content Brief]
[9]. de Bruin C, et al. An XRCC4 splice mutation associated with severe short stature, gonadal failure, and early-onset metabolic syndrome. J Clin Endocrinol Metab. 2015 May;100(5):E789-98. [Content Brief]
[10]. Fukuchi M, et al. Lysine 271 but not lysine 210 of XRCC4 is required for the nuclear localization of XRCC4 and DNA ligase IV. Biochem Biophys Res Commun. 2015 Jun 12;461(4):687-94. [Content Brief]
[11]. Roy S, et al. XRCC4/XLF Interaction Is Variably Required for DNA Repair and Is Not Required for Ligase IV Stimulation. Mol Cell Biol. 2015 Sep 1;35(17):3017-28. [Content Brief]
[12]. Zhang Q, et al. FBXW7 Facilitates Nonhomologous End-Joining via K63-Linked Polyubiquitylation of XRCC4. Mol Cell. 2016 Feb 4;61(3):419-433. [Content Brief]
[13]. Li Z, et al. The XRCC4 gene encodes a novel protein involved in DNA double-strand break repair and V(D)J recombination. Cell. 1995 Dec 29;83(7):1079-89. [Content Brief]
[14]. Koch CA, et al. Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV. EMBO J. 2004 Oct 1;23(19):3874-85. [Content Brief]
[15]. Mani RS, et al. Dual modes of interaction between XRCC4 and polynucleotide kinase/phosphatase: implications for nonhomologous end joining. J Biol Chem. 2010 Nov 26;285(48):37619-29. [Content Brief]
[16]. Brouwer I, et al. Sliding sleeves of XRCC4-XLF bridge DNA and connect fragments of broken DNA. Nature. 2016 Jul 28;535(7613):566-9. [Content Brief]
[17]. Ropars V, et al. Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joining. Proc Natl Acad Sci U S A. 2011 Aug 2;108(31):12663-8. [Content Brief]
[18]. Hammel M, et al. XRCC4 protein interactions with XRCC4-like factor (XLF) create an extended grooved scaffold for DNA ligation and double strand break repair. J Biol Chem. 2011 Sep 16;286(37):32638-50. [Content Brief]
[19]. Andres SN, et al. A human XRCC4-XLF complex bridges DNA. Nucleic Acids Res. 2012 Feb;40(4):1868-78. [Content Brief]
[20]. Normanno D, et al. Mutational phospho-mimicry reveals a regulatory role for the XRCC4 and XLF C-terminal tails in modulating DNA bridging during classical non-homologous end joining. Elife. 2017 May 13;6:. [Content Brief]
[21]. Recuero-Checa MA, et al. Electron microscopy of Xrcc4 and the DNA ligase IV-Xrcc4 DNA repair complex. DNA Repair (Amst). 2009 Dec 3;8(12):1380-9. [Content Brief]
[22]. Grawunder U, et al. Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells. Nature. 1997 Jul 31;388(6641):492-5. [Content Brief]
[23]. Berg E, et al. XRCC4 controls nuclear import and distribution of Ligase IV and exchanges faster at damaged DNA in complex with Ligase IV. DNA Repair (Amst). 2011 Dec 10;10(12):1232-42. [Content Brief]
[24]. Aceytuno RD, et al. Structural and functional characterization of the PNKP-XRCC4-LigIV DNA repair complex. Nucleic Acids Res. 2017 Jun 2;45(10):6238-6251. [Content Brief]
[25]. Maruoka M, et al. Caspase cleavage releases a nuclear protein fragment that stimulates phospholipid scrambling at the plasma membrane. Mol Cell. 2021 Apr 1;81(7):1397-1410.e9. [Content Brief]
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