Anti β actin clone c4

Manufactured by Merck Group

Sourced in United States

The Anti-β-actin clone C4 is a monoclonal antibody that specifically binds to the beta-actin protein, a ubiquitous cytoskeletal protein found in all eukaryotic cells. This antibody is commonly used in Western blotting, immunofluorescence, and other immunodetection techniques as a tool for the detection and quantification of beta-actin expression in various biological samples.

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Lab products found in correlation

Anti ubiquitin clone p4d1, by Santa Cruz Biotechnology (3 mentions) Anti ubiquitin clone fk2 and anti lamp1 clone ly1c6, by Enzo Life Sciences (2 mentions) Anti k48 linked polyubiquitin clone d9d5 and anti k63 linked polyubiquitin clone d7a11, by Cell Signaling Technology (2 mentions) Anti syntaxin 13 clone 151, by Synaptic Systems (2 mentions) Anti a tubulin clone b 5 1 2, by Merck Group (2 mentions) Anti eea1 clone 14, by BD (2 mentions) Ab200420, by Abcam (1 mentions) Mini protease inhibitor mixture, by Roche (1 mentions) Anti pyrin, by Adipogen (1 mentions) Transblot turbo midi size pvdf membranes, by Bio-Rad (1 mentions) Anti flag, by Merck Group (1 mentions) Anti flag m2 affinity gel, by Merck Group (1 mentions) Sodium fluoride, by Merck Group (1 mentions) Anti lin28a, by Abcam (1 mentions) Anti flag clone l5, by BioLegend (1 mentions) Anti cpsf73, by Fortis Life Sciences (1 mentions) Anti hur, by Santa Cruz Biotechnology (1 mentions) Anti hmga2, by GeneTex (1 mentions) Anti lin28b, by Cell Signaling Technology (1 mentions) Anti ras, by Abcam (1 mentions)

Close spelling variants of this product

β-actin (6886 citations) Anti-β-actin (3256 citations) Anti-actin (1282 citations) Anti-actin (clone C4, (31 citations) Anti-Actin C4 (12 citations) Clone C4 (9 citations) Actin (clone C4, (8 citations) β-actin (clone C4; (3 citations) Anti-β-actin (C4, (3 citations)

8 protocols using anti β actin clone c4

pH-sensitive GFP and AMPAR Imaging

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cDNAs encoding full-length pH-sensitive GFP, pHluorin-tagged GluA1 (pH-GluA1), and pH-GluA2 were subcloned into a vector downstream of chicken β-actin (CAG) promoter. C-terminal lysine to arginine mutants for both pH-GluA1 and pH-GluA2 were generated using the standard overlap extension PCR protocol.
Specific antibodies against GluA1 (4.9D), GluA2 (6A), GluA3 (JH4300), GluA4 (JH4303), and GFP (JH4030) were generated in the R.L.H. laboratory. The following antibodies were purchased from commercial sources: anti-ubiquitin clone P4D1 (Santa Cruz Biotechnology), anti-ubiquitin clone FK2 and anti-LAMP1 clone Ly1C6 (Enzo Lifesciences), anti-K48-linked polyubiquitin clone D9D5 and anti-K63-linked polyubiquitin clone D7A11 (Cell Signaling Technology), anti-EEA1 clone 14 (BD Transduction Laboratories), anti-syntaxin-13 clone 151.2 (Synaptic Systems), anti-a-tubulin clone B-5-1-2 (Sigma), anti-β-actin clone C4 (Millipore), and anti-PSD-95 clone K28/43 (NeuroMab). All drugs and chemicals were obtained from Tocris Biosciences or Ascent Scientific.

Widagdo J., Chai Y.J., Ridder M.C., Chau Y.Q., Johnson R.C., Sah P., Huganir R.L, & Anggono V. (2015). Activity-Dependent Ubiquitination of GluA1 and GluA2 Regulates AMPA Receptor Intracellular Sorting and Degradation. Cell reports, 10(5), 783-795.

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Immunoprecipitation and Western Blot Analysis of Pyrin

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Cells were lysed in 25 mM Tris–HCl, 150 mM NaCl, 1 mM EDTA, and 0.1% NP‐40 buffer containing Mini Protease Inhibitor Mixture (Roche) and sodium fluoride (Sigma) by a quick freezing and thawing step. Flag‐Pyrin was immuno‐precipitated using anti‐Flag M2 affinity gel (Sigma). Proteins were separated by SDS–PAGE on precast 4–15% acrylamide gels (Bio‐Rad) and transferred to TransBlot® Turbo™ Midi‐size PVDF membranes (Bio‐Rad). Antibodies used were mouse monoclonal anti‐FLAG^® (Sigma‐Aldrich, clone M2; 1:1,000 dilution), anti‐Pyrin (Adipogen, AL196, 1: 1,000 dilution), anti‐phospho S242 Pyrin (Abcam, ab200420; 1:1,000 dilution; Gao et al, 2016), and anti‐PKN1 (Becton Dickinson, BD 610687; 1:1,000 dilution). Cell lysates were reprobed with a mouse monoclonal antibody anti‐β‐actin (clone C4, Millipore; 1:5,000 dilution). Full Western blot images are presented in Source Data.

Magnotti F., Lefeuvre L., Benezech S., Malsot T., Waeckel L., Martin A., Kerever S., Chirita D., Desjonqueres M., Duquesne A., Gerfaud‐Valentin M., Laurent A., Sève P., Popoff M., Walzer T., Belot A., Jamilloux Y, & Henry T. (2019). Pyrin dephosphorylation is sufficient to trigger inflammasome activation in familial Mediterranean fever patients. EMBO Molecular Medicine, 11(11), e10547.

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Anti-Neuroserpin Antibody Generation

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Generation and affinity-purification of anti-neuroserpin goat polyclonal antibody has been previously described (Galliciotti et al. 2007 (link)). Commercially available antibodies included: Anti-synaptophysin (ab32594) and anti-SNAP25 (ab41455) from Abcam, anti-synapsin-I (D12G5) from Cell Signaling Technology, anti-PSD-95 (clone EP2652Y) and anti-β-actin (clone C4) from Millipore.

Reumann R., Vierk R., Zhou L., Gries F., Kraus V., Mienert J., Romswinkel E., Morellini F., Ferrer I., Nicolini C., Fahnestock M., Rune G., Glatzel M, & Galliciotti G. (2017). The serine protease inhibitor neuroserpin is required for normal synaptic plasticity and regulates learning and social behavior. Learning & Memory, 24(12), 650-659.

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pH-sensitive GFP and AMPAR Imaging

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Comprehensive Western Blot Antibody Panel

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Anti-hLin41 (R&D), anti-Lin28B (Cell Signaling Technology), anti-Lin28A (Abcam), anti-β-actin (clone C4, Millipore), anti-α-tubulin (clone TU-02, Santa Cruz Biotech), anti-CPSF73 (Bethyl Laboratories), anti-symplekin (BD Biosciences), anti-HuR (Santa Cruz Biotech), anti-Ras (Abcam), anti-eIF4GI [6 (link)], anti-FLAG (clone L5, BioLegend), and anti-HMGA2 (GeneTex) antibodies were used through the all western blot analysis.

Yin J., Kim T.H., Park N., Shin D., Choi H.I., Cho S., Park J.B, & Kim J.H. (2016). TRIM71 suppresses tumorigenesis via modulation of Lin28B-let-7-HMGA2 signaling. Oncotarget, 7(48), 79854-79868.

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Generation and Validation of Trak1 Antibody

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Rabbit polyclonal anti-Trak1 antibody was generated against the synthetic peptide corresponding to residues 935–953 of human Trak1 and was affinity-purified as previously described (Webber et al., 2008 (link)). Other primary antibodies used in this study include: anti-TOM20 (Santa Cruz); anti-Mfn1 (Abcam); anti-Mfn2 (ProteinTech Group, Inc.); anti-Miro1 (clone 4H4, Abnova); anti-Miro2 (ProteinTech Group, Inc); anti-Drp1 (Abcam); anti-GFP (B2, Santa Cruz); anti-Myc (9E10); anti-HSP60 (Stressgen); anti-GAPDH (Cell Signaling); and anti-β-actin (clone C4, Millipore). Horseradish-peroxidase-conjugated and FITC- or TRITC-conjugated secondary antibodies were from Jackson ImmunoResearch Laboratories.

Lee C.A., Chin L.S, & Li L. (2017). Hypertonia-linked protein Trak1 functions with mitofusins to promote mitochondrial tethering and fusion. Protein & Cell, 9(8), 693-716.

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Characterization of GluA1 Receptor Mutants

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The plasmids encoding full-length wild-type pH-GluA1 and the K868R and qKR mutants have been described previously (23 ). The pH-sensitive GFP (pHluorin) tag was inserted after the signal peptide sequence in the extracellular N-terminal region of GluA1. C-terminal serine to alanine or aspartate mutants for pH-GluA1 were generated using the standard overlap extension polymerase chain reaction protocol.
Specific antibodies against GluA1 (4.9D; 1:5,000) and GFP (JH4030; 1:1,000) were generated in the Huganir laboratory and have been characterized previously (23 ). The following antibodies were purchased from commercial sources: anti-ubiquitin clone P4D1 (Santa Cruz Biotechnology; 1:1,000) and clone FK2 (Enzo Life Sciences), anti-GluA1 phospho-Ser-831 (Millipore, AB5847; 1:2,500), anti-GluA1 phospho-Ser-845 (Millipore, AB5849; 1:2,500), anti-HA clone C29F4 (Cell Signaling Technology; 1:1,000), anti-synaptophysin clone 7.2 (Synaptic System; 1:10,000), and anti-β-actin clone C4 (Millipore; 1:10,000).

Guntupalli S., Jang S.E., Zhu T., Huganir R.L., Widagdo J, & Anggono V. (2017). GluA1 subunit ubiquitination mediates amyloid-β-induced loss of surface α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors. The Journal of Biological Chemistry, 292(20), 8186-8194.

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Immunoblotting of Stem Cell Markers

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The following antibodies were used: anti-ID1 (C-20, 1:200; Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti-IGF2 (clone S1F2, 1:5000; Millipore), anti-IGF1R (no. 9750; Cell Signaling Technology), anti-p-Akt (no. 4060; Cell Signaling Technology), anti-Sox2 (no. 3579; Cell Signaling Technology) and anti-β-actin (clone C4, 1:20 000; Millipore) antibodies.

Tominaga K., Shimamura T., Kimura N., Murayama T., Matsubara D., Kanauchi H., Niida A., Shimizu S., Nishioka K., Tsuji E.I., Yano M., Sugano S., Shimono Y., Ishii H., Saya H., Mori M., Akashi K., Tada K.I., Ogawa T., Tojo A., Miyano S, & Gotoh N. (2016). Addiction to the IGF2-ID1-IGF2 circuit for maintenance of the breast cancer stem-like cells. Oncogene, 36(9), 1276-1286.

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