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Rabbit anti phospho h2ax

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Rabbit anti-phospho-H2AX is a primary antibody that binds to the phosphorylated form of the histone variant H2AX. H2AX phosphorylation is an early cellular response to the presence of DNA double-strand breaks.

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Lab products found in correlation

Rabbit anti parp, by Cell Signaling Technology (2 mentions) Rabbit anti histone h3, by Cell Signaling Technology (1 mentions) Mouse anti phospho histone h3, by Cell Signaling Technology (1 mentions) Mouse anti p53, by Santa Cruz Biotechnology (1 mentions) Mouse anti actin, by Merck Group (1 mentions) Mouse anti p21, by BD (1 mentions) Duolink in situ red starter kit mouse rabbit, by Merck Group (1 mentions) Cycloheximide (chx), by Merck Group (1 mentions) Actinomycin d, by Merck Group (1 mentions) Rabbit anti 53bp1 4937, by Cell Signaling Technology (1 mentions) Nu7441, by Cayman Chemical (1 mentions) Tenovin 6, by Cayman Chemical (1 mentions) Az 20, by Cayman Chemical (1 mentions) Ku 60019, by Cayman Chemical (1 mentions) Nutlin 3, by Cayman Chemical (1 mentions) Palbociclib, by Selleck Chemicals (1 mentions) Pd0325901, by Selleck Chemicals (1 mentions) Mouse anti parp1, by Merck Group (1 mentions)

Spelling variants of this product

Phospho-H2AX (38 citations) Anti-H2AX (30 citations) Anti-phospho-H2AX (18 citations) Rabbit anti-H2AX (10 citations) Anti–phospho-histone H2AX (Ser 139) rabbit antibody (2 citations) Rabbit anti-phospho (Ser139)-histone H2AX (γH2AX) (2 citations) Anti‐phospho‐Histone H2AX (Ser139) rabbit Ab (1 citations)

5 protocols using rabbit anti phospho h2ax

1

Western Blot Analysis of Cell Cycle Regulators

Cited 1 time
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Antibodies used included mouse anti-Wee1, mouse anti-P53 (Santa Cruz Biotechnology, Santa Cruz, CA, U.S.A.), rabbit anti-phospho-CDK1 (Y15), rabbit anti-phospho-H2AX (S139), mouse anti-phospho-Histone H3 (S10), rabbit anti-Histone H3 (Cell Signaling Technology, Danvers, MA, U.S.A.), mouse anti-CDK1 (Millipore, Billerica, MA, U.S.A.), mouse anti-P21 (BD Biosciences, San Diego, CA, U.S.A.), and mouse anti-Actin (Sigma, St. Louis, MO, U.S.A.). Western blots were performed as previously described [13 (link)].
Pappano W.N., Zhang Q., Tucker L.A., Tse C, & Wang J. (2014). Genetic inhibition of the atypical kinase Wee1 selectively drives apoptosis of p53 inactive tumor cells. BMC Cancer, 14, 430.
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2

Proximity Ligation Assay for PARP1 and p97

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Proximity ligation assays were carried out with Duolink® In Situ Red Starter Kit Mouse/Rabbit (Sigma-Aldrich) according to the manufacturer’s protocol. The primary antibodies used were mouse anti-PARP1 (WH0000142M1-100UG), rabbit anti-PARP (Cell Signalling), mouse anti-p97 (ab11433) and rabbit anti-phospho-H2AX (Cell Signalling). The antibodies were used in 1:1500 dilution. Images were acquired on Marianas advanced spinning disk confocal microscope (3i) and analysed with a custom CellProfiler pipeline. Typically, several hundred nuclei were counted per condition from at least two independent biological repeats.
Krastev D.B., Li S., Sun Y., Wicks A.J., Hoslett G., Weekes D., Badder L.M., Knight E.G., Marlow R., Pardo M.C., Yu L., Talele T.T., Bartek J., Choudhary J.S., Pommier Y., Pettitt S.J., Tutt A.N., Ramadan K, & Lord C.J. (2022). The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin. Nature Cell Biology, 24(1), 62-73.
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3

Histological Analysis of Embryonic Tissue

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Histological analysis was performed on whole embryos fixed in neutral buffered formalin for 24 hr. The samples were then paraffin embedded, and 4 μm sections were cut before being stained with hematoxylin and eosin. For immunohistochemistry, samples were cut and stained as described previously (Langevin et al., 2011 (link)), using rabbit anti-phospho-H2AX (Cell Signaling, 2577, 1:50) and rabbit anti-cleaved caspase-3 (Cell Signaling, Asp175 9661L, 1:100).
Oberbeck N., Langevin F., King G., de Wind N., Crossan G.P, & Patel K.J. (2014). Maternal Aldehyde Elimination during Pregnancy Preserves the Fetal Genome. Molecular Cell, 55(6), 807-817.
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4

Investigating DNA Damage Response Pathways

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PD0325901and palbociclib were obtained from Selleckchem. Nutlin-3, tenovin-6, KU-60019, AZ-20, and NU-7441 were from Cayman. Rabbit anti-phospho-Rb (Ser807/811) (8516), rabbit anti-phospho-Rb (Ser807/811) pre-conjugated with Alexa 647 (8974), rabbit anti-p21 (2947), rabbit anti-p53 (2527), rabbit anti-53BP1 (4937) and rabbit anti-phospho-H2AX (9718) were from Cell Signaling Technology. Mouse anti-p21 (556430) was from BD Pharmingen, mouse anti-phospho-H2AX (05–636) was from EMD Millipore, and rabbit anti-cyclin D1 (RM-9104-S0) was from Thermo Scientific. Actinomycin D, cycloheximide and NCS were from Sigma-Aldrich.
Yang H.W., Chung M., Kudo T, & Meyer T. (2017). Competing memories of mitogen and p53 signalling control cell-cycle entry. Nature, 549(7672), 404-408.
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5

Quantification of PARP1 and p97 Interactions

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The PLA assays were carried out using a Duolink in situ red starter kit mouse/rabbit kit (Sigma-Aldrich) according to the manufacturer’s protocol. The primary antibodies used were: mouse anti-PARP1 (Sigma-Aldrich, WH0000142M1), rabbit anti-PARP (Cell Signaling), mouse anti-p97 (Abcam, ab11433) and rabbit anti-phospho-H2AX (Cell Signaling). The antibodies were used at a 1:1,500 dilution. Images were acquired on a Marianas advanced spinning disk confocal microscope (3i) and analysed using a custom CellProfiler pipeline. Typically, several hundred nuclei were counted per condition from at least two independent biological repeats.
Krastev D.B., Li S., Sun Y., Wicks A.J., Hoslett G., Weekes D., Badder L.M., Knight E.G., Marlow R., Pardo M.C., Yu L., Talele T.T., Bartek J., Choudhary J.S., Pommier Y., Pettitt S.J., Tutt A.N., Ramadan K, & Lord C.J. (2022). The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin. Nature Cell Biology, 24(1), 62-73.
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