HPA001334
Anti-LIG4 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
别名:
Anti-DNA ligase 4 antibody produced in rabbit, Anti-DNA ligase IV antibody produced in rabbit, Anti-Polydeoxyribonucleotide synthase [ATP] 4 antibody produced in rabbit
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Conjugate:
unconjugated
Clone:
polyclonal
Application:
immunohistochemistry
Species reactivity:
mouse, rat, human
Citations:
7
Technique(s):
immunohistochemistry: 1:200- 1:500
Uniprot accession no.:
产品名称
Anti-LIG4 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
product line
Prestige Antibodies® Powered by Atlas Antibodies
form
buffered aqueous glycerol solution
species reactivity
mouse, rat, human
technique(s)
immunohistochemistry: 1:200- 1:500
immunogen sequence
TYCVIAGSENIRVKNIILSNKHDVVKPAWLLECFKTKSFVPWQPRFMIHMCPSTKEHFAREYDCYGDSYFIDTDLNQLKEVFSGIKNSNEQTPEEMASLIADLEYRYSWDCSPLSMFRRHTVYLDSYA
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... LIG4(3981)
Application
Anti-LIG4 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem/physiol Actions
LIG4 (ligase IV) gene encodes a DNA ligase that links single-strand breaks in a double-stranded polydeoxynucleotide. The reaction is ATP-dependent. It is involved in the ligation step during non-homologous DNA end joining (NHEJ) and V(D)J recombination. NHEJ pathway repairs double-strand DNA breaks while V(D)J recombination involves the breakage and rejoining (dependent on NHEJ) of double-strand DNA.The protein forms a complex with the X-ray repair cross complementing protein 4 (XRCC4), which improves the joining activity of LIG4. This complex interacts with DNA-dependent protein kinase complex DNA-PK. This interaction is required for NHEJ. Defects in this gene cause LIG4 syndrome, characterized by immunodeficiency and developmental and growth delay.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Features and Benefits
Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.
Every Prestige Antibody is tested in the following ways:
Every Prestige Antibody is tested in the following ways:
- IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
- Protein array of 364 human recombinant protein fragments.
Immunogen
DNA ligase 4 recombinant protein epitope signature tag (PrEST)
Other Notes
Corresponding Antigen APREST78242
Physical form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Legal Information
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
10 - Combustible liquids
wgk
WGK 1
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
Emil Mladenov et al.
Nucleic acids research, 48(4), 1905-1924 (2019-12-14)
In vertebrates, genomic DNA double-strand breaks (DSBs) are removed by non-homologous end-joining processes: classical non-homologous end-joining (c-NHEJ) and alternative end-joining (alt-EJ); or by homology-dependent processes: gene-conversion (GC) and single-strand annealing (SSA). Surprisingly, these repair pathways are not real alternative options
Sohee Jun et al.
Nature communications, 7, 10994-10994 (2016-03-25)
Despite the implication of Wnt signalling in radioresistance, the underlying mechanisms are unknown. Here we find that high Wnt signalling is associated with radioresistance in colorectal cancer (CRC) cells and intestinal stem cells (ISCs). We find that LIG4, a DNA
M O'Driscoll et al.
Molecular cell, 8(6), 1175-1185 (2002-01-10)
DNA ligase IV functions in DNA nonhomologous end-joining and V(D)J recombination. Four patients with features including immunodeficiency and developmental and growth delay were found to have mutations in the gene encoding DNA ligase IV (LIG4). Their clinical phenotype closely resembles
Rebeka Eki et al.
Nucleic acids research, 48(21), e126-e126 (2020-10-18)
DNA double-strand breaks (DSBs) are highly cytotoxic lesions that can lead to chromosome rearrangements, genomic instability and cell death. Consequently, cells have evolved multiple mechanisms to efficiently repair DSBs to preserve genomic integrity. We have developed a DSB repair assay
U Grawunder et al.
Molecular cell, 2(4), 477-484 (1998-11-11)
Nonhomologous DNA end joining (NHEJ) is the major pathway for repairing double-strand DNA breaks. V(D)J recombination is a double-strand DNA breakage and rejoining process that relies on NHEJ for the joining steps. Here we show that the targeted disruption of
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