Anti p21 10355 1 ap

Manufactured by Proteintech

Sourced in China, United States

Anti-p21 (10355-1-AP) is a primary antibody that specifically recognizes the p21 protein. P21 is a cyclin-dependent kinase inhibitor that regulates cell cycle progression. This antibody can be used for applications such as Western blotting, immunohistochemistry, and immunofluorescence.

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Close spelling variants of this product

Anti-p21 (45 citations) P21 (10355-1-AP, (8 citations) Anti-TM (2 citations) Rabbit anti-p21 (10355-1-AP, (2 citations)

6 protocols using anti p21 10355 1 ap

Immunoprecipitation and Western Blot

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Anti-Flag (M2) and anti-c-Myc agarose, as well as anti-Flag M2 (F3165) mouse monoclonal antibody were purchased from Sigma (St. Louis, MO, USA). Anti-BCCIP (16043-1-AP) and anti-p21 (10355-1-AP) polyclonal antibodies were from Proteintech Group (Wuhan, China). Anti-YY1 (H414) (sc-1703 or sc-1703X) rabbit polyclonal antibody, anti-Myc (9E10, sc-40) mouse monoclonal antibody, rabbit total IgG (sc-2027), and mouse total IgG (sc-2025) were obtained from Santa Cruz Biotechnology (Dallas, TX, USA). Anti-p53 mouse monoclonal antibody was provided by Boster Group (BM0101, Wuhan, China). The ChIP grade anti-p53 mouse monoclonal antibody was from Abcam (ab1101, USA). Anti-p53S15P (RLP0205), anti-p53T18P (RLT0212), anti-p53S20P (RLT0206), anti-GADD45 (RLT1832), anti-Bax (RLT0456), and anti-Flag (RLG0004) rabbit polyclonal antibodies, Bcl2 (RLM3041) and anti-HA (RLM3003) mouse monoclonal antibodies were obtained from Ruiying (Suzhou, China). Anti-GAPDH (NM_002046, full length) polyclonal antibody and anti-BCCIP (NM_078468, residues 1-322) mouse polyclonal antibody were raised against bacterially expressed proteins (Jilin University, Changchun, China). 5-Fluorouracil (5FU) (F6627, Sigma) was dissolved in dimethyl sulfoxide (DMSO) and prepared at a 500 mM concentration for storage. The final concentration of 5FU in cell culture medium was 250 μM.

Sui Y., Wu T., Li F., Wang F., Cai Y, & Jin J. (2019). YY1/BCCIP Coordinately Regulates P53-Responsive Element (p53RE)-Mediated Transactivation of p21Waf1/Cip1. International Journal of Molecular Sciences, 20(9), 2095.

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Antibody Assays for Protein Interactions

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Anti-INO80 (24819-1-AP), anti-BCCIP (16043-1-AP), and anti-p21 (10355-1-AP) antibodies were purchased from Proteintech Group (Wuhan, China). Anti-YY1 (H414; sc-1703) and anti-α-Tubulin antibodies were obtained from Santa Cruz Biotechnology (Dallas, TX, USA). Anti-p53 mouse monoclonal antibody was provided by Boster Group (BM0101, Wuhan, China). Anti-Arp8 and anti-GAPDH were raised against bacterially expressed proteins (Jilin University).

Shah J.A., Miao Y., Chu J., Chen W., Zhao Q., Cai C., Khattak S., Wang F, & Jin J. (2023). Feedback Modulation between Human INO80 Chromatin Remodeling Complex and miR-372 in HCT116 Cells. International Journal of Molecular Sciences, 24(13), 10685.

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Antibodies for Chromatin and Signaling Analysis

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The antibodies anti-H3K9ac (#2594), anti-H3K27ac (#8173), anti-H3K56ac (#07-677-1S), anti-H4K8ac (#2594), anti-H4K12ac (#13944), anti-H4K16ac (#13534), anti-H3 (#4499), anti-H4 (#13919), anti-BRD4 (#13440), anti-Tom20 (#42406), anti-γ-H2AX (#80312), anti-H2AX (#7631), anti-p-TBK1(Cell #5483), anti-TBK1 (#3504), anti-p-IRF3 (#29047y), anti-IRF3 (#11904), anti-p-P65 (#3033), anti-P65 (#8242), anti-p-STAT1(#9167), anti-STAT1(#9172), anti-STING (#3337) and anti-p-P53 (#9286) were from Cell Signaling Technology; anti-cGAS (26416–1-AP), anti-P53 (10442-1-AP), anti-MDM2 (19058-1-AP) and anti-P21 (#10355-1-AP) were from Proteintech; anti-dsDNA (MAB1293) was from Millipore; and anti-actin (A1978) was from Sigma. Antiserum against PRV gE was generated by immunization of mice with purified recombinant gE.

Wang J., Li G.L., Ming S.L., Wang C.F., Shi L.J., Su B.Q., Wu H.T., Zeng L., Han Y.Q., Liu Z.H., Jiang D.W., Du Y.K., Li X.D., Zhang G.P., Yang G.Y, & Chu B.B. (2020). BRD4 inhibition exerts anti-viral activity through DNA damage-dependent innate immune responses. PLoS Pathogens, 16(3), e1008429.

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Western Blot Analysis of Cellular Proteins

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We added 50 μg proteins from cell lysates to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) gel and transferred them to a polyvinylidene difluoride (PVDF) membrane (MilliporeSigma, Burlington, Massachusetts, US) for blotting with antibodies against CHK1(ab40866), IP10 (ab214668), Fas (ab133619) and Eg5 (ab181981; all from Abcam, Cambridge, UK); as well as with Phospho-CHK1-Ser317 (12302S), Phospho-CHK1-Ser345 (2348S) or BIM (2933T; all from Cell Signaling Technologies [CST], Danvers, Massachusetts, US). Additionally, we used anti-GAPDH (10494-2-AP), anti-BubR1 (11504-2-AP), anti-cyclin B1 (55004-1-AP), anti-UBE2S (14115-1-AP) and anti-p21 (10355-1-AP) from Proteintech (Rosemont, Illinois, US), as well as anti-MSX2 (A2017) from ABclonal (Woburn, Massachusetts, US) and anti-CENPF (DF2310) from Affinity Biotech (Cincinnati, Ohio, US), for immunoreactivity (overnight at 4° C) which was visualized with an enhanced chemiluminescence kit (MilliporeSigma).

Xu W., Huang M., Guo J., Zhang H., Wang D., Liu T., Liu H., Chen S., Gao P, & Mu K. (2020). The Role of CHK1 Varies with the Status of Oestrogen-receptor and Progesterone-receptor in the Targeted Therapy for Breast Cancer. International Journal of Biological Sciences, 16(8), 1388-1402.

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Western Blot Analysis of Protein Expression

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Western blot was performed as previously described [56 (link)]. Briefly, proteins from tissues or cultured cells were extracted in lysis buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 1% Triton X-100, and 0.25% sodium deoxycholate). Samples were separated by 10% SDS-PAGE and transferred onto PVDF membranes. Membranes were blocked with 5% non-fat milk powder and then incubated overnight at 4 °C with each primary antibody. Primary antibodies used in this study included anti-Caveolin-1 (sc-894, Santa Cruz, CA, USA), anti-GAPHD (sc-25778, Santa Cruz), anti-a-Tubulin (2144, Cell Signaling Technology), anti-p-CREB (9198s, Cell Signaling Technology, Danvers, MA, USA), anti-p53 (2521p, Cell Signaling Technology), anti-p21 (10355-1-AP, Proteintech, Wuhan, China), anti-ZO1 (ab221547, Abcam, Cambridge, UK). The membranes were incubated with HRP-conjugated secondary antibody at room temperature for 1 h. ECL chemiluminescent kits (Milipore) were used for detecting the signals.

Song Z., Li B., Li M., Luo J., Hong Y., He Y., Chen S., Yang Z., Liang C, & Yang Z. (2022). Caveolin-1 Regulation and Function in Mouse Uterus during Early Pregnancy and under Human In Vitro Decidualization. International Journal of Molecular Sciences, 23(7), 3699.

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Protein Isolation and Western Blot Analysis

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After the experiment, the brain tissues and pancreas tissues of rats were collected, and the total proteins were extracted by radio immunoprecipitation analysis (RIPA) and lysis buffer solution. The protein concentration was determined by bicinchoninic acid (BCA) method. A total of 200 μg protein samples were separated by 12% sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The isolated proteins were transferred to a polyvinylidene fluoride membrane that had been activated by methanol and blocked by 5% skim milk and dried at room temperature for at least 1 h. The primary antibodies were then incubated overnight at 4°C. The primary antibodies for incubation included anti-CD11b (66519-1-Ig, 1:2000, Proteintech, USA), anti-CD86 (13395-1-AP, 1:1000, Proteintech, USA), anti-cleaved-caspase 3 (19677-1-AP, 1:1000, Proteintech, USA), anti-p21 (10355-1-AP, 1:1000, Proteintech, USA), anti-P16 (10883-1-AP, 1:1000, Bioss, China), and anti-b-actin (60008-1-Ig, 1:5000, Proteintech, USA). They were then incubated with anti-mouse IgG (SA00001-1, 1:5000, Proteintech, USA) and antirabbit IgG (SA00001-2, 1:6000, Proteintech, USA) at 37 °C for 90 min. Chemiluminescence (Millipore, USA) was visualized and analysed using imaging software (GE Healthcare, Life Sciences, USA).

Li X., He J., Li X., Li Y., Zhou Y, & Cai S. (2021). Neu-P11 - a novel melatonin receptor agonist, could improve the features of type-2 diabetes mellitus in rats. Endokrynologia Polska, 72(6).

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