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Merck

HPA006801

Sigma-Aldrich

Anti-XRCC4 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Szinonimák:

Anti-DNA-repair protein XRCC4, Anti-X-ray repair cross-complementing protein 4

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
Human Protein Atlas-szám:
NACRES:
NA.41
konjugátum:
unconjugated
application:
IF
IHC
klón:
polyclonal
faj reaktivitás:
human
citations:
8
technika/technikák:
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:500-1:1000

biológiai forrás

rabbit

Minőségi szint

konjugátum

unconjugated

antitest forma

affinity isolated antibody

antitest terméktípus

primary antibodies

klón

polyclonal

termékcsalád

Prestige Antibodies® Powered by Atlas Antibodies

Forma

buffered aqueous glycerol solution

faj reaktivitás

human

fejlettebb validálás

RNAi knockdown
orthogonal RNAseq
recombinant expression
Learn more about Antibody Enhanced Validation

technika/technikák

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:500-1:1000

immunogén szekvencia

KCVSAKEALETDLYKRFILVLNEKKTKIRSLHNKLLNAAQEREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTDIAPSRKRRQRMQRNLGTEPKMAPQENQLQEK

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... XRCC4(7518)

Immunogén

DNA-repair protein XRCC4 recombinant protein epitope signature tag (PrEST)

Alkalmazás

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biokémiai/fiziológiai hatások

XRCC4 (X-ray repair complementing defective repair in Chinese hamster cells 4) is mainly involved in the XRCC4-dependent DNA double-strand repair pathway. Mono-ubiquitinated XRCC4 binds to the ligase for the formation of DNA ligase IV-XRCC4 complex. Generally, ligase is unstable in nature, but in the presence of mono-ubiquitinated XRCC4, it becomes stable during ligation. The complex directly acts on the duplex DNA end part and bridging between the duplex DNA molecules and complementary but non-ligatable ends. Finally, through protein-protein interactions, DNA ligase IV-XRCC4 complex facilitates the intermolecular ligation in the presence of DNA-dependent protein kinase (DNA-PK).

Tulajdonságok és előnyök

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:
  • 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.

Kapcsolódás

Corresponding Antigen APREST71076

Fizikai forma

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Jogi információk

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Jogi nyilatkozat

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.

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Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Válasszon a legfrissebb verziók közül:

Analitikai tanúsítványok (COA)

Lot/Batch Number

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Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

Dylan A Reid et al.
Proceedings of the National Academy of Sciences of the United States of America, 112(20), E2575-E2584 (2015-05-06)
Nonhomologous end-joining (NHEJ) is a major repair pathway for DNA double-strand breaks (DSBs), involving synapsis and ligation of the broken strands. We describe the use of in vivo and in vitro single-molecule methods to define the organization and interaction of
Gaetano Ivan Dellino et al.
Nature genetics, 51(6), 1011-1023 (2019-05-22)
It is not clear how spontaneous DNA double-strand breaks (DSBs) form and are processed in normal cells, and whether they predispose to cancer-associated translocations. We show that DSBs in normal mammary cells form upon release of paused RNA polymerase II
S A Nick McElhinny et al.
Molecular and cellular biology, 20(9), 2996-3003 (2000-04-11)
Genetic experiments have determined that Ku, XRCC4, and ligase IV are required for repair of double-strand breaks by the end-joining pathway. The last two factors form a tight complex in cells. However, ligase IV is only one of three known
Gaetano Ivan Dellino et al.
Nature genetics, 51(6), 1011-1023 (2019-05-22)
It is not clear how spontaneous DNA double-strand breaks (DSBs) form and are processed in normal cells, and whether they predispose to cancer-associated translocations. We show that DSBs in normal mammary cells form upon release of paused RNA polymerase II
L Chen et al.
The Journal of biological chemistry, 275(34), 26196-26205 (2000-06-16)
The DNA-dependent protein kinase (DNA-PK), consisting of Ku and the DNA-PK catalytic subunit (DNA-PKcs), and the DNA ligase IV-XRCC4 complex function together in the repair of DNA double-strand breaks by non-homologous end joining. These protein complexes are also required for

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