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Anti p21 waf1 cip1 12d1

Manufactured by Cell Signaling Technology
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Anti-p21 Waf1/Cip1 (12D1) is a rabbit monoclonal antibody that recognizes the p21 Waf1/Cip1 protein. p21 Waf1/Cip1 is a cyclin-dependent kinase inhibitor that plays a role in cell cycle regulation.

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Lab products found in correlation

Anti β actin, by Cell Signaling Technology (2 mentions) Anti β tubulin, by Cell Signaling Technology (1 mentions) Complete ultra protease inhibitor, by Roche (1 mentions) Phenyl methyl sulfonyl fluoride (pmsf), by Merck Group (1 mentions) Anti v5 tag, by Thermo Fisher Scientific (1 mentions) Clarity western ecl substrate, by Bio-Rad (1 mentions) Fusion fx documentation system, by Vilber (1 mentions) Anti γh2ax ser139, by Cell Signaling Technology (1 mentions) Bca protein assay, by Merck Group (1 mentions) Clarity ecl detection kit, by Bio-Rad (1 mentions) Anti β actin, by Merck Group (1 mentions) Irdye 800cw goat anti mouse igg, by LI COR (1 mentions) Irdye 800cw goat anti rabbit igg, by LI COR (1 mentions) Irdye 680rd goat anti mouse igg, by LI COR (1 mentions) Peroxidase conjugated donkey anti rabbit igg h l, by Jackson ImmunoResearch (1 mentions) Amersham ecl peroxidase linked sheep anti mouse igg, by GE Healthcare (1 mentions) Anti flag m2 antibody, by Merck Group (1 mentions) Goat anti rabbit igg, by LI COR (1 mentions) Anti hrgfp, by Agilent Technologies (1 mentions) Anti ha, by Santa Cruz Biotechnology (1 mentions)

Spelling variants of this product

Anti-p21 (226 citations) P21 Waf1/Cip1 (79 citations) Anti-p21 Waf1/Cip1 (25 citations) P21 Waf1/Cip1 (12D1) (20 citations) Anti-p21 (12D1) (3 citations) Anti-p21/WAF1 (3 citations) Anti-p21 Waf1/Cip1 (12D1) antibodies (2 citations)

5 protocols using anti p21 waf1 cip1 12d1

1

Analyzing ZC3H12B Protein Expression

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HeLa cells were transfected with V5-ZC3H12B wild-type or aspartic acid to alanine mutant expression vectors or empty control vector (pcDNA3) in 12-well plates. Twenty-four hours after transfection the cells were lysed in RIPA buffer (25 mM Tris-HCl pH 7.6, 150 mM NaCl, 1% NP-40, 1% sodium deoxycholate, 0.1% SDS with cOmplete ULTRA protease inhibitors [Roche] and 1 mM PMSF [Sigma-Aldrich]) and 20–30 µg of protein extracts were analyzed by western blot. For the doxycycline inducible cell lines, the cells were seeded in 12-well plates and the following day the cells were treated with 1 µg/mL doxycycline for recombinant protein expression. After induction the cells were lysed and analyzed as described above for HeLa cells. The following antibodies were used: anti-V5 tag (R96025, Thermo Scientific), anti-p21 Waf1/Cip1 (12D1, Cell Signaling Technology), anti-β-actin, anti-β-tubulin, anti-mouse-HRP and anti-rabbit HRP (Cell Signaling). Luminescence was detected using Clarity Western ECL Substrate (Bio-Rad) and recorded using the Fusion-Fx documentation system (Vilber Lourmat).
Wawro M., Wawro K., Kochan J., Solecka A., Sowinska W., Lichawska-Cieslar A., Jura J, & Kasza A. (2019). ZC3H12B/MCPIP2, a new active member of the ZC3H12 family. RNA, 25(7), 840-856.
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2

Protein Expression Analysis by Western Blotting

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Cells were pelleted and lysed using RIPA buffer (10 mM Tris-Cl (pH 8.0), 1 mM EDTA, 1% Triton X-100, 0.1% sodium deoxycholate, 0.1% SDS, 140 mM NaCl, 1 mM PMSF). Lysates were sonicated and protein concentration was determined using BCA protein assay (Sigma). 30 μg of total proteins were loaded on 12% SDS–PAGE gel and separated by electrophoresis. Protein were transferred on PVDF membrane, dried and blotted overnight in 5% BSA TBS-T at 4 °C using primary antibodies (Abcam anti-SMARCD3: ab171075; Santa Cruz anti-beta-Actin (C-4): sc-47778; Millipore anti-γH2AX (Ser139): 05–636; Cell Signaling anti- p21WAF1/CIP1 (12D1): 2947). Afterwards, membranes were incubated with secondary antibodies for one hour at room temperature and developed using Clarity ECL Detection Kit (Bio-Rad).
Tropée R., de la Peña Avalos B., Gough M., Snell C., Duijf P.H, & Dray E. (2020). The SWI/SNF subunit SMARCD3 regulates cell cycle progression and predicts survival outcome in ER+ breast cancer. Breast cancer research and treatment, 185(3), 601-614.
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3

Western Blot Analysis of HIV-1 and Cell Proteins

Cited 1 time
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Cells were lysed in buffer containing 50 mM Tris–HCl (pH 8.0), 150 mM NaCl, 4 mM EDTA, 1% Nonidet (N) P-40, 0.1% sodium dodecyl sulfate (SDS), 1 mM dithiothreitol (DTT) and 1 mM phenylmethylsulfonyl fluoride (PMSF). Supernatants from these lysates were subjected to SDS-polyacrylamide gel electrophoresis, followed by immunoblot analysis using anti-HIV-1 p24 (65-005; Bioacademia, Osaka, Japan), anti-p21Waf1/Cip1 (12D1) (#2947; Cell Signaling Technology, Inc., Danvers, MA 01923, USA), anti-p21 [EPR362] (ab 109520; Abcam), anti-β-actin (A5441; Sigma, Saint Louis, MI, USA), anti-HA (HA-7; Sigma), anti-HA (12CA5; Santa Cruz), anti-FLAG antibody (M2; Sigma), anti-S6 ribosomal protein (5G10; Cell Signaling Technology), anti-GAPDH (GA1R, Pierce Biotechnology), anti-hrGFP (#240141, Agilent Technologies), or anti-hORF1p (SE-6798) (65 (link)) as primary antibodies. We used peroxidase-conjugated Donkey anti-Rabbit IgG (H+L) (Jackson ImmunoResearch), Amersham ECL peroxidase-linked Sheep anti-Mouse IgG (GE Healthcare), IRDye 800CW Goat anti-Rabbit IgG, IRDye 800CW Goat anti-Mouse IgG, IRDye 680RD Goat anti-Rabbit IgG or IRDye 680RD Goat anti-Mouse IgG (LI-COR Biosciences) as secondary antibodies.
Kawano K., Doucet A.J., Ueno M., Kariya R., An W., Marzetta F., Kuroki M., Turelli P., Sukegawa S., Okada S., Strebel K., Trono D, & Ariumi Y. (2018). HIV-1 Vpr and p21 restrict LINE-1 mobility. Nucleic Acids Research, 46(16), 8454-8470.
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4

Autophagy and Cell Cycle Regulation

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The reagents used in this study were as follows: bafilomycin A1 (MedChemExpress, HY-100558), 3-Methyladenine (MedChemExpress, HY-19312), SC 79 (MedChemExpress, HY-18749) and Chloroquine (Enzo Life Sciences 51005-CQC). The antibodies used in this study were as follows: anti LC3A/B (1:1,000, Cell Signaling Technologies, 12741), anti SQSTM1/p62 (1:1,000, Cell Signaling Technologies, 5114), anti cyclin D1 (1:1,000, Cell Signaling Technologies, 55506), anti cyclin E2 (1:1,000, Cell Signaling Technologies, 4132), anti Phospho-Akt (Ser473) (1:1,000 Cell Signaling Technologies, 4060), anti Phospho-PI3 Kinase p85 (Tyr458)/p55 (Tyr199), (1:1,000, Cell Signaling Technologies, 4228), anti Phospho-mTOR (Ser2448) (1:1,000 Cell Signaling Technologies,5536T), anti Akt (1:1,000, Cell Signaling Technologies, 9272), anti p21 Waf1/Cip1 (12D1) (1:1,000, Cell Signaling Technologies, 2947), anti ATG5 (1:5,000, Proteintech Group, 10181-2-AP), anti PI3KR1 (1:5,000, Proteintech Group, 60225-1-Ig), anti mTOR (1:5,000, Proteintech Group, 66888-1-Ig), anti b-actin (1:1,000, Cell Signaling Technologies, 3700), HRP, goat anti mouse IgG polyclone (1:10,000, Abbkine, A21010), HRP, goat anti rabbit IgG polyclone (1:10,000, Abbkine, A21020).
Wang Y., Yuan Y., Wang C., Wang B., Zou W., Zhang N, & Chen X. (2022). Theabrownins Produced via Chemical Oxidation of Tea Polyphenols Inhibit Human Lung Cancer Cells in vivo and in vitro by Suppressing the PI3K/AKT/mTOR Pathway Activation and Promoting Autophagy. Frontiers in Nutrition, 9, 858261.
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5

Evaluation of LAT1 Inhibitor JPH203 Effects

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The LAT1 inhibitor JPH203 was kindly provided by J-Pharma (Kanagawa, Japan). The following antibodies were used: anti-phospho-p70 S6k, anti-p21 Waf1/Cip1 (12D1), HRP-conjugated secondary antibodies (Cell Signaling Technology, Beverly, MA, USA), anti-p70 S6k, and anti-actin (Santa Cruz Biotechnology, Dallas, TX, USA). The Western Lightning Plus-ECL chemiluminescence detection kit was purchased from PerkinElmer (Waltham, MA, USA). The cell ATP assay reagent was obtained from Toyo Ink (Tokyo, Japan).
Bo T., Kobayashi S., Inanami O., Fujii J., Nakajima O., Ito T, & Yasui H. (2021). LAT1 inhibitor JPH203 sensitizes cancer cells to radiation by enhancing radiation-induced cellular senescence. Translational Oncology, 14(11), 101212.
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