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Anti beta actin clone ac 15

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Sourced in Germany, United States

Anti-beta Actin (Clone AC-15) is a monoclonal antibody that specifically recognizes the beta-actin isoform of the actin protein. Actin is a ubiquitous and highly conserved cytoskeletal protein found in all eukaryotic cells. This antibody is a useful tool for the detection and quantification of beta-actin in various applications, such as Western blotting, immunohistochemistry, and immunocytochemistry.

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Lab products found in correlation

Anti mlh1 g168 728, by BD (4 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (4 mentions) Anti pms2 a16 4, by BD (3 mentions) Nitrocellulose, by LI COR (2 mentions) Ripa buffer, by Bio-Rad (2 mentions) Sample buffer, by Bio-Rad (2 mentions) Anti sox2 d6d9 rabbit monoclonal, by Cell Signaling Technology (2 mentions) Donkey anti rabbit irdye 680, by LI COR (2 mentions) Odyssey infrared scanner, by LI COR (2 mentions) Irdye 800cw goat anti mouse, by LI COR (2 mentions) β mercaptoethanol, by Merck Group (2 mentions) Anti phospho akt substrate 23c8d2, by Cell Signaling Technology (2 mentions) Anti p mlh1, by Cell Signaling Technology (2 mentions) Anti fluorescence labeled anti rabbit irdye800cw, by LI COR (2 mentions) Anti fluorescence labeled anti mouse irdye680lt, by LI COR (2 mentions) Anti bcl 2 2876, by Cell Signaling Technology (1 mentions) Anti phospho akt 9271, by Cell Signaling Technology (1 mentions) Anti pten 9559, by Cell Signaling Technology (1 mentions) Oligonucleotide, by Merck Group (1 mentions) Pegfp c1 plasmid, by Takara Bio (1 mentions)

7 protocols using anti beta actin clone ac 15

1

Western Blot Analysis of Tbx3, PTEN, Bcl-2, and Phospho-Akt

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For western blotting analysis, anti-Tbx3 antibody was purchased from Novus Biologicals (H00006926-A01; Littleton, CO, USA); anti-PTEN (9559), anti-Bcl-2 (2876) and anti-phospho-Akt (9271) were all purchased from Cell Signaling Biotechnology (Danvers, MA, USA). Anti-flag tag antibody (F7425) and anti-beta-actin (clone AC-15) were from Sigma-Aldrich (St. Louis, MO, USA). Synthetic miR-206 mimic, antagomiR-206 (αmiR-206) and miR scrambled control (NC) were purchased from Qiagen (Valencia, CA, USA). pMIR-REPORT Luciferase vector and control vector were purchased from Applied Biological Materials (ABM MT-h25249; Richmond, BC, Canada), SMART pool: ON-TARGETplus, Tbx3-siRNA (LU-012197-00-0005) and set of four individual siRNA (LU-012197-000002) were purchased from Dharmacon (Lafayette, CO, USA). Human Tbx3 flag-tagged cDNA (RC220990) was from OriGene Technologies, Inc. (Rockville, MD, USA).
Amir S., Simion C., Umeh-Garcia M., Krig S., Moss T., Carraway KL I.I.I, & Sweeney C. (2016). Regulation of the T-box transcription factor Tbx3 by the tumour suppressor microRNA-206 in breast cancer. British Journal of Cancer, 114(10), 1125-1134.
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2

Western Blot Analysis of SOX2 Expression

Cited 1 time
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Whole-cell lysates of ≥100,000 cells were used per lane. Western blotting was performed as previously reported [2 (link)]. Briefly, cells were rinsed with cold PBS and scraped into RIPA buffer supplemented with protease inhibitors, sonicated twice, and re-suspended in 4X sample buffer (BioRad; Hercules, CA) supplemented with 10% beta-mercaptoethanol (Sigma-Aldrich; St. Louis MO). The Pierce BCA protein assay kit (Thermo Fisher Scientific; Grand Island, NY) was used to determine protein concentration. Protein (60 μg) was electrophoresed on 10% SDS-polyacrylamide gels and transferred to nitrocellulose (Odyssey, LI-COR Biosciences; Lincoln, NE) overnight at 4°C. Membranes were blocked overnight in 5% non-fat milk in TBS at 4°C. Primary antibodies used were: anti-SOX2 (D6D9 rabbit monoclonal, Cell Signaling Technologies) and anti-beta actin (clone AC-15, Sigma-Aldrich). Secondary antibodies were goat anti-mouse IRDye 800 CW or donkey anti-rabbit IRDye 680 (LI-COR Biosciences), and images were captured using an infrared Odyssey scanner (LI-COR Biosciences).
de Wet L., Williams A., Gillard M., Kregel S., Lamperis S., Gutgesell L.C., Vellky J.E., Brown R., Conger K., Paner G.P., Wang H., Platz E.E., De Marzo A.M., Mu P., Coloff J.L., Szmulewitz R.Z, & Vander Griend D.J. (2022). SOX2 Mediates Metabolic Reprogramming of Prostate Cancer Cells. Oncogene, 41(8), 1190-1202.
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3

Antibody Characterization for MLH1 Analysis

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Anti-MLH1 (G168-728) and anti-PMS2 (A16-4) were purchased from Pharmingen (BD Biosciences, Heidelberg, Germany), anti-beta Actin (Clone AC-15) was from Sigma-Aldrich (Munich, Germany). Anti-phospho-AKT-substrate (23C8D2), used for the detection of phosphorylation of MLH1 at amino acid position serine 477 and hereinafter referred to as anti-p-MLH1, was obtained from Cell Signaling (New England Biolabs GmbH, Frankfurt, Germany). Anti-MLH1 (N-20), anti-CK2α (D-10), and anti-Lamin β (C-20) were from Santa Cruz (Santa Cruz Biotechnology, Heidelberg, Germany). Anti-MLH1 (ab74541) (Abcam, Cambridge UK) and anti-Adaptin γ (clone 88/Adaptin γ (RUO)) were from BD Biosciences (BD Biosciences, Heidelberg, Germany).
Anti-fluorescence-labeled anti-rabbit IRDye800CW and anti-fluorescence-labeled anti-mouse IRDye680LT were from LI-COR (LI-COR Biosciences GmbH, Bad Homburg, Germany).
Ulreich K., Firnau M.B., Tagscherer N., Beyer S., Ackermann A., Plotz G, & Brieger A. (2022). High Expression of Casein Kinase 2 Alpha Is Responsible for Enhanced Phosphorylation of DNA Mismatch Repair Protein MLH1 and Increased Tumor Mutation Rates in Colorectal Cancer. Cancers, 14(6), 1553.
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4

Antibody Immunoblotting Protocols

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Anti-SPTAN1 (C-11), anti-Lamin B (C-20) and anti-MSH2 (H-300) were obtained from Santa Cruz Biotechnology (Santa Cruz, CA), anti-MLH1 (G168-728) as well as anti-gamma Adaptin (88) were from Pharmingen (BD Biosciences, United States), anti-beta Actin (Clone AC-15) was purchased from Sigma (Sigma-Aldrich, USA) and anti-SPTAN1 (MAB1622) was from Millipore (Millipore, USA).
The pcDNA3.1+/MLH1, pcDNA3.1+/PMS2 and pcDNA3.1+/MSH2 expression plasmids were described previously [27 (link)]. Full length SPTAN1 cDNA was generated from total RNA of human lymphocytes and subcloned into the eukaryotic expression vector pcDNA3.1- via the KpnI/XhoI restriction sites.
All plasmids were confirmed by sequencing and reading frames were corrected using site-directed mutagenesis, if necessary. All oligonucleotides were purchased from Sigma-Aldrich (Munich, Germany).
Hinrichsen I., Ernst B.P., Nuber F., Passmann S., Schäfer D., Steinke V., Friedrichs N., Plotz G., Zeuzem S, & Brieger A. (2014). Reduced migration of MLH1 deficient colon cancer cells depends on SPTAN1. Molecular Cancer, 13, 11.
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5

Immunoblotting for Phospho-MLH1 Detection

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Anti-MLH1 (G168-728) and anti-PMS2 (A16-4) were purchased from Pharmingen (BD Biosciences, Heidelberg, Germany). Anti-beta Actin (Clone AC-15) was from Sigma-Aldrich (Munich, Germany). Anti-phospho-AKT-substrate (23C8D2), used for the detection of phosphorylation of MLH1 at amino acid position serine 477 and hereinafter referred to as anti-p-MLH1, was obtained from Cell Signaling (New England Biolabs GmbH, Frankfurt, Germany).
Anti-fluorescence-labeled anti-mouse IRDye680LT and anti-fluorescence-labeled anti-rabbit IRDye800CW were from LI-COR (LI-COR Biosciences GmbH, Bad Homburg, Germany).
Firnau M.B., Plotz G., Zeuzem S, & Brieger A. (2023). Key role of phosphorylation sites in ATPase domain and Linker region of MLH1 for DNA binding and functionality of MutLα. Scientific Reports, 13, 12503.
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6

Western Blot Analysis of SOX2 Expression

Cited 1 time
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Whole-cell lysates of ≥100,000 cells were used per lane. Western blotting was performed as previously reported [2 (link)]. Briefly, cells were rinsed with cold PBS and scraped into RIPA buffer supplemented with protease inhibitors, sonicated twice, and re-suspended in 4X sample buffer (BioRad; Hercules, CA) supplemented with 10% beta-mercaptoethanol (Sigma-Aldrich; St. Louis MO). The Pierce BCA protein assay kit (Thermo Fisher Scientific; Grand Island, NY) was used to determine protein concentration. Protein (60 μg) was electrophoresed on 10% SDS-polyacrylamide gels and transferred to nitrocellulose (Odyssey, LI-COR Biosciences; Lincoln, NE) overnight at 4°C. Membranes were blocked overnight in 5% non-fat milk in TBS at 4°C. Primary antibodies used were: anti-SOX2 (D6D9 rabbit monoclonal, Cell Signaling Technologies) and anti-beta actin (clone AC-15, Sigma-Aldrich). Secondary antibodies were goat anti-mouse IRDye 800 CW or donkey anti-rabbit IRDye 680 (LI-COR Biosciences), and images were captured using an infrared Odyssey scanner (LI-COR Biosciences).
de Wet L., Williams A., Gillard M., Kregel S., Lamperis S., Gutgesell L.C., Vellky J.E., Brown R., Conger K., Paner G.P., Wang H., Platz E.E., De Marzo A.M., Mu P., Coloff J.L., Szmulewitz R.Z, & Vander Griend D.J. (2022). SOX2 Mediates Metabolic Reprogramming of Prostate Cancer Cells. Oncogene, 41(8), 1190-1202.
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7

Characterization of MMR Protein Variants

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Anti-MLH1 (G168-728) and anti-PMS2 (A16-4) were purchased from Pharmingen (BD Biosciences, Heidelberg, Germany), anti-beta Actin (Clone AC-15) was from Sigma-Aldrich (Munich, Germany). Anti-phospho-AKT-substrate (23C8D2), hereinafter The pcDNA3.1+/MLH1 and pcDNA3.1+/PMS2 expression plasmids were described previously [12] . In addition, the MLH1-variants MLH1 S477A , MLH1 D478A and MLH1 E480A were generated by site-directed mutagenesis (for detailed primer information see supplementary table 1) and overexpressed in HEK293T cells.
All plasmids were confirmed by sequencing. All oligonucleotides were purchased from Sigma-Aldrich (Munich, Germany). pEGFP_C1 plasmid (negative control plasmid for the MMR assay) was purchased from Clontech Laboratories.
Weßbecher I.M., Hinrichsen I., Funke S., Oellerich T., Plotz G., Zeuzem S., Grus F.H., Biondi R.M, & Brieger A. (2018). DNA mismatch repair activity of MutLα is regulated by CK2-dependent phosphorylation of MLH1 (S477). Molecular carcinogenesis, 57(12).
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