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p-Artemis (S516) pAb

p-Artemis (S516) pAb

Cat no: BS4644


Supplier: Bioworld Technology, Inc.
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Distinct DNA repair pathways minimize the consequences of mutagenic events. Reactive oxygen species (ROS) are highly reactive atoms with an unpaired electron that are conducive to double-strand DNA breaking events. Artemis, named after the Greek goddess for the protection of children, is one of the major proteins contributing to the preservation of double-strand breaks in DNA by cutting away the damaged parts of the DNA, which allows the strands to rejoin. Artemis is a single-strand-specific 5' to 3' exonuclease that forms a complex with the 469 kDa DNA-dependent protein kinase (DNA-PKcs). DNA-PKcs phosphorylates Artemis, and Artemis acquires endonucleolytic activity on 5' and 3' overhangs and hairpins. These activities are essential for V(D)J recombination and for the 5' and 3' overhang processing in nonhomologous DNA end joining.
Catalogue number: BS4644
Reactivities: Human, Mouse, Rat
Hosts: Rabbit
Applications: Immunohistochemistry, Western Blot
Size: 100ug/100ul
Swiss prot: Q96SD1
Dilutions: WB: 1:500~1:1000 IHC: 1:50~1:200
Form: liquid
Storage buffer: 1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.
Concentration: 1ug/ul
Antigen: Synthetic phosphopeptide derived from human Artemis around the phosphorylation site of Serine 516.
Species: p-Artemis (S516) pAb detects endogenous levels of Protein artemis only when phosphorylated at Ser516.
Molecular weight: ~ 78 kDa
Purity: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Storage temp: Store at 4 degrees C short term. Aliquot and store at -20 degrees C long term. Avoid freeze-thaw cycles.
Alternative names: Protein artemis; DNA cross-link repair 1C protein; Protein A-SCID; SNM1 homolog C; hSNM1C; SNM1-like protein; DCLRE1C; ARTEMIS; ASCID; SCIDA; SNM1C
Additional info: For research use only, not for use in diagnostic procedure.

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