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AB185815

Anti-DNA Ligase III/LIG3 antibody

5

(2 Reviews)

|

(7 Publications)

Rabbit Polyclonal DNA Ligase III/LIG3 antibody. Suitable for WB, IP and reacts with Human samples. Cited in 7 publications. Immunogen corresponding to Recombinant Fragment Protein within Human LIG3.

View Alternative Names

DNA ligase 3, DNA ligase III, Polydeoxyribonucleotide synthase [ATP] 3, LIG3

2 Images
Immunoprecipitation - Anti-DNA Ligase III/LIG3 antibody (AB185815)
  • IP

Supplier Data

Immunoprecipitation - Anti-DNA Ligase III/LIG3 antibody (AB185815)

DNA Ligase III/LIG3 was immunoprecipitated from 200μg Jurkat cells using 1μg ab185815. Western blot was performed on the immunoprecipitate using ab185815 at 1/1000 dilution.  Lane 1 : Input (Jurkat cell lysate) Lane 2 : Control IgG Lane 3 : ab185815 IP in Jurkat cell lysate

All lanes:

Immunoprecipitation - Anti-DNA Ligase III/LIG3 antibody (ab185815) at 1 µg

All lanes:

Jurkat cell lysate

Observed band size: 113 kDa

false

Western blot - Anti-DNA Ligase III/LIG3 antibody (AB185815)
  • WB

Supplier Data

Western blot - Anti-DNA Ligase III/LIG3 antibody (AB185815)

Blocking buffer : 3% nonfat dry milk in TBST

All lanes:

Western blot - Anti-DNA Ligase III/LIG3 antibody (ab185815) at 1/1000 dilution

Lane 1:

BT474 at 25 µg

Lane 2:

SW480 at 25 µg

Lane 3:

HeLa at 25 µg

Lane 4:

HT-29 at 25 µg

Lane 5:

Jurkat at 25 µg

Secondary

All lanes:

HRP Goat Anti-Rabbit IgG (H+L) at 1/1000 dilution

Predicted band size: 113 kDa

Observed band size: 113 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IP, WB

applications

Immunogen

Recombinant Fragment Protein within Human LIG3. The exact immunogen used to generate this antibody is proprietary information.

P49916

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"}, "IP" : {"fullname" : "Immunoprecipitation", "shortname":"IP"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/2000", "WB-species-notes": "<p></p>", "IP-species-checked": "testedAndGuaranteed", "IP-species-dilution-info": "1/50 - 1/200", "IP-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.3 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

DNA Ligase III also known as LIG3 or Lig 3 is an enzyme that plays a central role in DNA repair by catalyzing the joining of DNA strands. Mechanically it facilitates the ligation step in the DNA repair process sealing nicks in the DNA backbone. This ligase has a sizing mass of approximately 103 kDa. It is expressed widely in human cells with a high concentration in tissues with active DNA repair needs such as testes and ovaries. Ligase acts in various subcellular locations including the nucleus and mitochondria with distinct isoforms functioning in these compartments.
Biological function summary

DNA Ligase III is significant in maintaining genomic stability. It often operates as part of multi-protein complexes interacting especially with XRCC1 during base excision repair (BER). It ensures the continuity of DNA strands after damage-induced breaks are processed. LIG3 also has a pivotal function in the mitochondria where it is involved in repair and replication of mitochondrial DNA therefore preserving mitochondrial genome integrity.

Pathways

DNA Ligase III is an integral part of the DNA repair pathways particularly the base excision repair (BER) and single-strand break repair (SSBR) pathways. In the BER pathway LIG3 collaborates closely with other proteins like XRCC1 to mend damaged DNA by filling in missing nucleotides and sealing nicks. It also plays a role in non-homologous end joining (NHEJ) though this is more dominantly accomplished by DNA Ligase IV. These pathways are important for correcting oxidative damage and abasic sites that can disrupt the DNA structure.

DNA Ligase III has associations with certain syndromes and cancers. Mutations or malfunctions in this enzyme can lead to ataxia-telangiectasia-like disorder owing to impaired DNA repair processes. Additionally LIG3 expression is often evaluated in the context of cancerous cells where aberrant repair processes could promote tumor progression. A connection with XRCC1 another key player in the repair machinery is critical as XRCC1 mutations may magnify the impact of LIG3 deficiencies contributing to disease pathology.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Isoform 3 functions as a heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as a DNA ligase in mitochondrial base-excision DNA repair (PubMed : 10207110, PubMed : 24674627).
See full target information LIG3

Publications (7)

Recent publications for all applications. Explore the full list and refine your search

Nature 621:415-422 PubMed37674080

2023

Polθ is phosphorylated by PLK1 to repair double-strand breaks in mitosis.

Applications

Unspecified application

Species

Unspecified reactive species

Camille Gelot,Marton Tibor Kovacs,Simona Miron,Emilie Mylne,Alexis Haan,Liza Boeffard-Dosierre,Rania Ghouil,Tatiana Popova,Florent Dingli,Damarys Loew,Josée Guirouilh-Barbat,Elaine Del Nery,Sophie Zinn-Justin,Raphael Ceccaldi

International journal of molecular sciences 24: PubMed37569794

2023

CSB Regulates Pathway Choice in Response to DNA Replication Stress Induced by Camptothecin.

Applications

Unspecified application

Species

Unspecified reactive species

Nicole L Batenburg,John R Walker,Xu-Dong Zhu

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 10:e2206896 PubMed36814305

2023

circCIMT Silencing Promotes Cadmium-Induced Malignant Transformation of Lung Epithelial Cells Through the DNA Base Excision Repair Pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Meizhen Li,Wei Chen,Jinjin Cui,Qiuyi Lin,Yufei Liu,Huixian Zeng,Qiuhan Hua,Yihui Ling,Xiaodi Qin,Yindai Zhang,Xueqi Li,Tianshu Lin,Lihua Huang,Yiguo Jiang

Nature 606:930-936 PubMed35477155

2022

Breakage of cytoplasmic chromosomes by pathological DNA base excision repair.

Applications

Unspecified application

Species

Unspecified reactive species

Shangming Tang,Ema Stokasimov,Yuxiang Cui,David Pellman

EMBO reports 21:e49076 PubMed32096305

2020

Human RAP1 specifically protects telomeres of senescent cells from DNA damage.

Applications

Unspecified application

Species

Unspecified reactive species

Liudmyla Lototska,Jia-Xing Yue,Jing Li,Marie-Josèphe Giraud-Panis,Zhou Songyang,Nicola J Royle,Gianni Liti,Jing Ye,Eric Gilson,Aaron Mendez-Bermudez

Molecular cell 74:466-480.e4 PubMed30930055

2019

TOP2β-Dependent Nuclear DNA Damage Shapes Extracellular Growth Factor Responses via Dynamic AKT Phosphorylation to Control Virus Latency.

Applications

Unspecified application

Species

Unspecified reactive species

Hui-Lan Hu,Lora A Shiflett,Mariko Kobayashi,Moses V Chao,Angus C Wilson,Ian Mohr,Tony T Huang

Genome biology 19:37 PubMed29548335

2018

Mutational signatures reveal the role of RAD52 in p53-independent p21-driven genomic instability.

Applications

Unspecified application

Species

Unspecified reactive species

Panagiotis Galanos,George Pappas,Alexander Polyzos,Athanassios Kotsinas,Ioanna Svolaki,Nickolaos N Giakoumakis,Christina Glytsou,Ioannis S Pateras,Umakanta Swain,Vassilis L Souliotis,Alexandros G Georgakilas,Nicholas Geacintov,Luca Scorrano,Claudia Lukas,Jiri Lukas,Zvi Livneh,Zoi Lygerou,Dipanjan Chowdhury,Claus Storgaard Sørensen,Jiri Bartek,Vassilis G Gorgoulis
View all publications

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