H2A.X Antikörper

Antigen: H2A.X

Klonalität: Polyklonal

Wirt: Kaninchen

Reaktivität: Human

Applikation: Western Blot (WB), Immunfluoreszenz (IF)

Produktnummer: ABIN160889

Produktbeschreibung

Immunogen: Recominant (partial), N-terminal

Format: Purified

Isotyp: IgG  (Passende Sekundärantikörper)

Klon: Poly6133

Beschreibung: H2A.X is a 14 kD basal histone and a member of the H2 histone family. This nuclear protein is synthesized in the G1 and S phase of the cell cycle and is known to be important for recombination between immunoglobulin switch regions. H2A.X becomes phosphorylated on serine 139 after double-stranded DNA breaks. Phosphorylated H2A.X promotes DNA repair and maintains genomic stability. The Poly6133 antibody has been shown to be useful for Western blotting and immunofluorescence of human H2A.X. Distribution: Nuclear Function: Phosphorylated H2AX promotes DNA repair and maintains genomic stability. Important for recombination between immunoglobulin switch regions Modifications: Phosphorylation on Ser139 after double-stranded DNA breaks Synonyms: H2A.x, H2a/x, Histone 2A, Histone 2A.X Regulation: Synthesized in G1 and S-phase of cell cycle Structure: Basal histone, member of the H2 histone family, 14 kD

Anwendungen

Applikationshinweise: Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 10 µl per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.

Reinigung: The antibody was purified by antigen-affinity chromatography.

Buffer: This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide and 50% glycerol.

Lagerung: Upon receipt, store frozen at -20° C.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Bilder

Hela cells were fixed in 4% paraformaldehyde , washed in PBS, and permeabilized using 0.5% Triton X-100 for 5 minutes prior to antibody staining. Cells were incubated with a 1:50 dilution of H2A.X antibody (Poly6133) for 1 hr, washed twice using 0.1% Triton X-100 in PBS and incubated with goat anti-rabbit conjugated to Alexa Fluor(R) 488 (top panel). After washing twice in 0.1% Triton X-100 in PBS, cells were mounted and examined on a fluorescent scope. DAPI stained cells are shown as a control (bottom panel). 100 X magnification. Jurkat nuclear extract was resolved by electrophoresis, transferred to nitrocellulose and probed with rabbit anti-H2A.X antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.

Jurkat nuclear extract was resolved by electrophoresis, transferred to nitrocellulose and probed with rabbit anti-H2A.X antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.

Jurkat nuclear extract was resolved by electrophoresis, transferred to nitrocellulose and probed with rabbit anti-H2A.X antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.

Publikationen

Publikationen: Mannironi, Bonner, Hatch: "H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signals." in: Nucleic acids research, Vol. 17, Issue 22, pp. 9113-26, 1990 (PubMed).

Celeste, Petersen, Romanienko et al.: "Genomic instability in mice lacking histone H2AX." in: Science (New York, N.Y.), Vol. 296, Issue 5569, pp. 922-7, 2002 (PubMed).

Bassing, Chua, Sekiguchi et al.: "Increased ionizing radiation sensitivity and genomic instability in the absence of histone H2AX." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 12, pp. 8173-8, 2002 (PubMed).

Reina-San-Martin, Difilippantonio, Hanitsch et al.: "H2AX is required for recombination between immunoglobulin switch regions but not for intra-switch region recombination or somatic hypermutation." in: The Journal of experimental medicine, Vol. 197, Issue 12, pp. 1767-78, 2003 (PubMed).