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Pser345 chk1

Manufactured by Cell Signaling Technology
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Sourced in United Kingdom, United States

PSer345 CHK1 is an antibody that recognizes the phosphorylated form of Checkpoint Kinase 1 (CHK1) at serine 345. CHK1 is a key regulator of the cell cycle and DNA damage response pathways. Phosphorylation of CHK1 at serine 345 is an important activation event that occurs in response to DNA damage or replication stress.

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Lab products found in correlation

Pthr68 chk2, by Cell Signaling Technology (2 mentions) Gapdh, by Merck Group (1 mentions) Chk1 pser296, by Cell Signaling Technology (1 mentions) Pser727 stat3, by Cell Signaling Technology (1 mentions) Total parp, by Cell Signaling Technology (1 mentions) Total caspase 3, by Cell Signaling Technology (1 mentions) P stat3 tyr705, by Cell Signaling Technology (1 mentions) C myc, by Cell Signaling Technology (1 mentions) Cleaved parp, by Cell Signaling Technology (1 mentions) Mcl 1, by Cell Signaling Technology (1 mentions) Bcl 2, by Cell Signaling Technology (1 mentions) Cleaved caspase 3, by Cell Signaling Technology (1 mentions) β actin, by Cell Signaling Technology (1 mentions) Nitrocellulose, by Cytiva (1 mentions) Anti chk1, by Cell Signaling Technology (1 mentions) Enhanced chemi luminescence (ecl), by Cell Signaling Technology (1 mentions) Anti β actin a5060, by Merck Group (1 mentions) Okadaic acid, by Merck Group (1 mentions) P ser824 kap 1, by Fortis Life Sciences (1 mentions) P h2ax ser139, by Merck Group (1 mentions)

Close spelling variants of this product

Rabbit anti-CHK1 pSer345

5 protocols using pser345 chk1

1

Western Blot Analysis of DNA Repair Proteins

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Western blots were carried out on 40 µg of protein extracted with NTEN (20 mM Tris at pH 8, 150 mM NaCl, 1 mM EDTA, 0.5% NP-40) plus protease and phosphatase inhibitors. All of the antibodies were incubated overnight at 4°C in 2% milk. The antibodies used were rabbit anti-Rad50 polyclonal, rabbit anti-Nbs1 polyclonal, and rabbit anti-Mre11 polyclonal previously described (49 (link)), ATM (Cell Signaling), RPA32 pSer4/Ser8 (Bethyl Laboratories), Chk1 (C9358, Sigma), Chk1 pSer345 (Cell Signaling), AID (50 (link))), GAPDH (6C5, Millipore) and Smc1 (Cell Signaling).
Balestrini A., Nicolas L., Yang-lott K., Guryanova O.A., Levine R.L., Bassing C.H., Chaudhuri J, & Petrini J.H. (2015). Defining ATM-independent Functions of the Mre11 Complex with a Novel Mouse Model. Molecular cancer research : MCR, 14(2), 185-195.
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2

Comprehensive Protein Expression Analysis

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Antibodies (Ab) against Chk1, Chk1-pSer296, Chk1-pSer317, Chk1-pSer345, p21, beta-Actin, H2AX, H2AX-pSer139, total PARP, cleaved-PARP, total caspase-3, cleaved-caspase-3, c-Myc, Bcl-2, Mcl-1, STAT3-pSer727, and STAT3-pTyr705 were purchased from Cell Signaling Technology. Anti-NFκB Ab was from Santa Cruz Biotechnology. Anti-p53 Ab (DO-1) was a gift from Dr. Borivoj Vojtesek (Masaryk Memorial Cancer Institute, Brno). Anti-rabbit and anti-mouse secondary antibodies were purchased from DakoCytomation. Anti-Ki-67-PE Ab and appropriate isotype control were purchased from BioLegend.
Zemanova J., Hylse O., Collakova J., Vesely P., Oltova A., Borsky M., Zaprazna K., Kasparkova M., Janovska P., Verner J., Kohoutek J., Dzimkova M., Bryja V., Jaskova Z., Brychtova Y., Paruch K, & Trbusek M. (2016). Chk1 inhibition significantly potentiates activity of nucleoside analogs in TP53-mutated B-lymphoid cells. Oncotarget, 7(38), 62091-62106.
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3

Cell Lysis and Protein Analysis

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Whole-cell extracts were prepared as described previously.44 (link) The cell lysis buffer was supplemented with 500 nM okadaic acid (Merck Chemicals, VWR International, Beeston, UK) when samples were used to analyse Aurora kinase sites of phosphorylation. Proteins were separated by SDS-PAGE and blotted onto nitrocellulose (Schleicher & Schuell). Proteins were detected using the enhanced chemiluminiscence detection system (ECL, Amersham) according to the manufacturer's recommendations using anti-CHK1 (#2345), pAurora: Phospho-Aurora A (Thr288)/Aurora B (Thr232)/Aurora C (Thr198) (#2914), p21 (#2947), pSer345 CHK1 (#2348), CHK1 (#2360), pThr68 CHK2 (#2661), CHK2 (#2662), pTyr15 CDK1 (#9111) from Cell Signaling, Hitchin, UK; anti-CDC45 (sc-20685), CDK1 (sc-54), Cyclin B1 (sc-245), pSer10 H3 (sc-8656), p53 (sc-126) from Santa Cruz Biotechnology (Wembley, UK) and anti-RPA34 (NA19L) from Calbiochem (Feltham, UK); or anti-β-actin (A-5060) from Sigma-Aldrich (Poole, UK).
Zuazua-Villar P., Rodriguez R., Gagou M.E., Eyers P.A, & Meuth M. (2014). DNA replication stress in CHK1-depleted tumour cells triggers premature (S-phase) mitosis through inappropriate activation of Aurora kinase B. Cell Death & Disease, 5(5), e1253-.
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4

Protein Extraction and Western Blotting for DNA Damage Signaling

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For total protein extract preparation, AMLMLL cells were collected upon treatment with ATRi (5 μM for 6 h) or HU (2 mM for 2 h), washed once with PBS and lysed in UREA buffer (8 M urea, 1 % Chaps, Tris-HCl 50 mM, pH 8.0) for 30 min at 4°C with agitation. Samples were resolved by SDS-PAGE and analysed by standard western blotting techniques. The following primary antibodies were used: p-Ser345 Chk1 (Cell Signaling), p-Ser4/Ser8 RPA32 (Bethyl), p-Ser139 H2AX (Millipore), H2AX (Abcam), p-SMC1 (Monoclonal Antibody Unit, CNIO), p-Ser824 KAP-1 (Bethyl) and PARP1 (Cell Signaling). Alexa Fluor 680- or 800- conjugated secondary antibodies (Life Technologies) were used for detection with a LI-COR Odyssey infrared imaging system (LI-COR Biosciences).
Morgado-Palacin I., Day A., Murga M., Lafarga V., Anton M.E., Tubbs A., Chen H.T., Ergan A., Anderson R., Bhandoola A., Pike K.G., Barlaam B., Cadogan E., Wang X., Pierce A.J., Hubbard C., Armstrong S.A., Nussenzweig A, & Fernandez-Capetillo O. (2016). Targeting the kinase activities of ATR and ATM exhibits therapeutic potential in a mouse model of MLL-rearranged AML. Science signaling, 9(445), ra91.
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5

Immunofluorescence Staining of Cytoskeletal Proteins

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Acetylated α-tubulin (Sigma-Aldrich, St. Louis, MO, USA, #T7451), tyrosylated α-tubulin (Genetex, Irvine, CA, USA, #GTX76511), β-tubulin (Sigma-Aldrich, #T5201), KIF11 (Abcam, Cambridge, MA, USA, #ab51976), vinculin (Sigma-Aldrich, #V9131), pTyr397-PTK2 (Thermo Fisher Scientific, Waltham, MA, USA #700255), α-adaptin (Thermo Fisher Scientific, #MA1-064), γ-H2AX (Genetex, #GTX127340; Cell Signaling Technology, Danvers, MA, USA, #9718), pSer345-CHK1 (Cell Signaling Technology, #2348), pThr68-CHK2 (Cell Signaling Technology, #2197), and NDC80 (Abcam, #ab3613).
Chien J.Y., Tsen S.D., Chien C.C., Liu H.W., Tung C.Y, & Lin C.H. (2016). αTAT1 downregulation induces mitotic catastrophe in HeLa and A549 cells. Cell Death Discovery, 2, 16006-.
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