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AB213658

Non-Homologous End Joining (H2A.X, gamma H2A.X pS139, DNA Ligase IV, Ku70, Ku80) Antibody Panel

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Non-Homologous End Joining (H2A.X, gamma H2A.X pS139, DNA Ligase IV, Ku70, Ku80) Antibody Panel (ab213658) is part of our antibody panels range. Abcam offers high-quality biological reagents and tools including antibodies, proteins, assays, cell lines and lysates.

View Alternative Names

G22P1, XRCC6, DNA repair protein Ku70, 5'-deoxyribose-5-phosphate lyase Ku70, 70 kDa subunit of Ku antigen, ATP-dependent DNA helicase 2 subunit 1, ATP-dependent DNA helicase II 70 kDa subunit, CTC box-binding factor 75 kDa subunit, DNA repair protein XRCC6, Lupus Ku autoantigen protein p70, Thyroid-lupus autoantigen, X-ray repair complementing defective repair in Chinese hamster cells 6, X-ray repair cross-complementing protein 6, 5'-dRP lyase Ku70, CTC75, CTCBF, Ku70, TLAA, H2AFX, H2AX, Histone H2AX, H2a/x, Histone H2A.X, G22P2, XRCC5, DNA repair protein Ku80, 86 kDa subunit of Ku antigen, ATP-dependent DNA helicase 2 subunit 2, ATP-dependent DNA helicase II 80 kDa subunit, CTC box-binding factor 85 kDa subunit, DNA repair protein XRCC5, Ku80, Ku86, Lupus Ku autoantigen protein p86, Nuclear factor IV, Thyroid-lupus autoantigen, X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining), X-ray repair cross-complementing protein 5, CTC85, CTCBF, TLAA, H2AFX, H2AX, Histone H2AX, H2a/x, Histone H2A.X, H2AS139p, H2AXS139p, H2A.XS139p, γh2ax, DNA ligase 4, DNA ligase IV, Polydeoxyribonucleotide synthase [ATP] 4, LIG4

Key facts

Target

XRCC6

target

Product details

ab213658 is a Non Homologous End Joining Panel designed for the detection and characterization of key proteins involved in DNA double strand break (DSB) repair by non-homologous end joining (NHEJ). Histone H2A.X is phosphorylated on S139, termed gamma H2A.X, at sites of DNA damage. DNA DSB repair by NHEJ requires Ku70/Ku80 heterodimer binding to the DSB, as well as DNA Ligase IV for ligation of DNA ends.

This panel contains 5 recombinant rabbit monoclonal antibodies. They are provided as a sampler panel to allow you to easily evaluate each in your applications.

The panel contains:

- Rabbit monoclonal anti-Histone H2A.X antibody [EPR895] - ChIP Grade (ab124781)

- Rabbit monoclonal anti-gamma H2A.X (phospho S139) antibody [EP854(2)Y] - ChIP Grade (ab81299)

- Rabbit monoclonal anti-DNA Ligase IV/LIG4 antibody [EPR16531] (ab193353)

- Rabbit monoclonal anti-Ku70 antibody [EPR4027] (ab92450)

- Rabbit monoclonal anti-Ku80 antibody [EPR3468] (ab80592)

For guidelines on how to use each antibody within the panel, please consult the individual datasheet for each antibody.

designed to provide you with a variety of trial-size antibodies in a convenient and cost-effective format.

What's included?

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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
-20°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Ku70 and Ku80 together with DNA Ligase IV (LIG4) and Histone H2A.X play significant roles in maintaining genomic stability especially through the non-homologous end joining pathway. Ku70 also known as XRCC6 is a 70 kDa protein and Ku80 or XRCC5 is approximately 80 kDa. Both proteins are ubiquitously expressed meaning they are found in various cell types. These proteins form a heterodimer complex with DNA Ligase IV that recognizes and aligns broken DNA ends facilitating repair. Histone H2A.X variants including gamma H2A.X become phosphorylated upon DNA damage and serve as a signal for recruiting repair machinery to the double-strand breaks.
Biological function summary

Ku70 and Ku80 act as a DNA-binding complex that is important in double-strand break repair via the non-homologous end joining mechanism. The Ku heterodimer associates with DNA Ligase IV in a multiprotein complex to bridge and ligate broken DNA strands. Histone H2A.X including its phosphorylated form gamma H2A.X marks sites of DNA damage. The H2A.X variants contribute to chromatin remodeling making the DNA accessible to repair proteins and maintaining genomic integrity.

Pathways

Non-homologous end joining is one critical pathway where Ku70 and Ku80 are involved. This pathway operates independently of a homologous template and is essential for repairing DNA double-strand breaks. Another related pathway is the cell cycle checkpoint signaling where gamma H2A.X's phosphorylation helps signal and stall the cell cycle allowing time for repair. In these pathways Ku proteins and DNA Ligase IV work alongside proteins such as DNA-PKcs and XRCC4 to ensure effective DNA repair.

Disruptions in the non-homologous end joining pathway connect to cancer development and immunodeficiencies. Defects in Ku70 Ku80 or DNA Ligase IV function can lead to genomic instability contributing to the onset of various cancers. Mutations in these proteins also relate to conditions like severe combined immunodeficiency (SCID) as ineffective DNA repair impairs lymphocyte development. These connections highlight the critical roles these proteins play in disease prevention.

Product protocols

Target data

DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with XRCC5 (Ku80), creating the Ku70 : Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends (PubMed : 11493912, PubMed : 20493174, PubMed : 33854234, PubMed : 34352203, PubMed : 9742108). This pathway ensures the rapid repair of cytotoxic and mutagenic DSBs and contributes to the generation of diversity in T-cell receptors and antibodies through mechanisms such as V(D)J recombination (PubMed : 9742108). Likely acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), catalyzing the beta-elimination of the 5'-deoxyribose-5-phosphate at abasic sites near DSBs. This activity cleans the termini of abasic sites, a common form of nucleotide damage, preparing broken ends for ligation (PubMed : 20383123). It may also possess 3'-5' DNA helicase activity, although this has not been confirmed in vivo, and its physiological significance remains unclear (PubMed : 7957065). Beyond DNA repair, the protein contributes to telomere maintenance (PubMed : 29490055). It is also implicated in transcriptional regulation, acting as a cofactor for various transcription factors (PubMed : 12145306, PubMed : 8621488). It plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed : 28712728). Can also bind RNAs and recruits PRKDC to a wide range of cellular RNAs, including the U3 small nucleolar RNA, playing a role in the biogenesis of ribosomal RNAs (PubMed : 32103174). Additionally, it negatively regulates apoptosis by interacting with BAX, sequestering it from the mitochondria, and may possess deubiquitination activity targeting BAX (PubMed : 15023334, PubMed : 18362350, PubMed : 35545041).
See full target information XRCC6

Additional targets

H2AX phospho S139,LIG4,XRCC5,H2AX

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