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Actin mab1501r

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Actin (MAB1501R) is a monoclonal antibody that recognizes the actin protein, a key structural component of the cytoskeleton in eukaryotic cells. The antibody can be used for the detection and localization of actin in various applications, such as immunohistochemistry, immunocytochemistry, and Western blotting.

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Lab products found in correlation

Odyssey scanner, by LI COR (3 mentions) Geneticin 1 10 phenanthroline monohydrate, by Merck Group (2 mentions) Anti alkaline phosphatase monoclonal antibody clone 8b6, by Merck Group (2 mentions) Pacs 2 sirna, by Qiagen (2 mentions) Pacs 2 antibody 19508 1 ap, by Proteintech (2 mentions) Pegfr ab40815, by Abcam (2 mentions) Egfr 06 847, by Merck Group (2 mentions) Adam9 af949, by R&D Systems (2 mentions) Adam17 mab9301, by R&D Systems (2 mentions) Green fluorescent protein expression plasmid, by Takara Bio (2 mentions) Complete edta free inhibitor cocktail, by Roche (2 mentions) Halt phosphatase inhibitor cocktail, by Thermo Fisher Scientific (2 mentions) Interferin transfection reagent, by Polyplus Transfection (2 mentions) Sc 1541, by Santa Cruz Biotechnology (2 mentions) Protease inhibitor cocktail, by Merck Group (2 mentions) Phosphatase inhibitor cocktail 2, by Merck Group (2 mentions) Phosphatase inhibitor cocktail 3, by Merck Group (2 mentions) Ab5714, by Abcam (1 mentions) Chemiluminescence kit, by Merck Group (1 mentions) Bcl2 associated x (bax), by Agilent Technologies (1 mentions)

Spelling variants of this product

MAB1501R (56 citations) β-actin (MAB1501R) (4 citations) Anti-actin (Mab1501R; (4 citations) Anti-actin antibody (MAB1501R) (4 citations)

12 protocols using actin mab1501r

1

Western Blot Analysis of Apoptosis Regulators

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After two washings with cold PBS, cells were lysed in ice-cold lysis buffer (SDS 1% EDTA 10 mM; Tris-HCl pH8,1 50 mM; protease inhibitors, Na3VO4 1 mM, NaF 100 × ) and extracts were sonicated. Protein extracts were separated by SDS-PAGE, transferred onto a PVDF membrane (Millipore, Billerica, MA, USA) and revealed with a chemiluminescence kit (Millipore). Presented Western-Blot are representative of three independent experiments. Following antibodies were used: actin (MAB1501R, Millipore), β-tubulin (T0198, Sigma), BAX (A3533, Dako), BCL-xL (1018-1, Epitomics), cytochrome c (BD-Pharmingen San Diego, CA, USA), MCL-1 (sc-819, Santa Cruz Biotechnologies, Santa Cruz, CA, USA), NOXA (ALX-804-408, Enzo Life Science, New York, NY, USA), PUMA (12450, Cell Signalling), p21 (2947, Cell Signalling), p53 (#554294, BD-Pharmigen). The above antibodies against BAX, BCL-xL and p53 were also used for immunoprecipitations, as those against BAX 6A7 (ab5714, Abcam, Cambridge, UK) and FLAG-tag (F1804, Sigma).
Le Pen J., Laurent M., Sarosiek K., Vuillier C., Gautier F., Montessuit S., Martinou J.C., Letaï A., Braun F, & Juin P.P. (2016). Constitutive p53 heightens mitochondrial apoptotic priming and favors cell death induction by BH3 mimetic inhibitors of BCL-xL. Cell Death & Disease, 7(2), e2083-.
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2

Protein Expression Analysis in Cells

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p53 (Sc-6243), p21 (Sc-756), MDM2 (Sc-5304), RAD51 (Sc-8349) and STAT-1 (Sc-346) (Santa Cruz biotechnology, Inc), cyclin D2 (3741) and caspase 1 (3866) (Cell Signaling technologies), and actin (MAB1501R) (Millipore, USA).
Palayoor S.T., John-Aryankalayil M., Makinde A.Y., Falduto M.T., Magnuson S.R, & Coleman C.N. (2014). Differential Expression of Stress and Immune Response Pathway Transcripts and miRNAs in Normal Human Endothelial Cells Subjected to Fractionated or Single-Dose Radiation. Molecular cancer research : MCR, 12(7), 1002-1015.
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3

PACS-2 Regulation of ADAM17-Mediated EGFR Signaling

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PMA and BB-94 were from Calbiochem. Geneticin, 1,10-phenanthroline monohydrate, MISSION Universal Negative Control siRNA #1, and anti-alkaline phosphatase monoclonal antibody (clone 8B6) were from Sigma-Aldrich. HALT Phosphatase Inhibitor Cocktail was from Thermo Scientific. Complete EDTA-free inhibitor cocktail was from Roche. Interferin transfection reagent was from PolyPlus, and siGENOME non-targeting siRNA pool #2, SMARTpool PACS-2 and ADAM17 siRNAs were from Dharmacon (Thermo Scientific). We additionally used PACS-2 siRNA from Qiagen and pooled three siRNAs (PACS2_6, PACS2_7 and PACS2_9). Recombinant murine TNF-α was from Strathmann Biotec AG. PACS-2 antibody (19508-1-AP) was from Proteintech. ADAM17 (ab39162), ADAM17 (ab2051), MT1-MMP (ab38971), ADAM10 (ab1997), and pEGFR (ab40815) antibodies were from Abcam. PACS-1 antibody 17703 and PACS-2 antibody 18193 were previously described53 (link),54 (link). Actin (MAB1501R) and EGFR (06–847) antibodies were from Millipore. ADAM9 (AF949), and ADAM17 (MAB9301) antibodies were from R&D Systems. PACS-2-HA expression plasmid was in a pcDNA.3 backbone40 (link) (Invitrogen), and green fluorescent protein (GFP) expression plasmid was from Clontech.
Dombernowsky S.L., Samsøe-Petersen J., Petersen C.H., Instrell R., Hedegaard A.M., Thomas L., Atkins K.M., Auclair S., Albrechtsen R., Mygind K.J., Fröhlich C., Howell M., Parker P., Thomas G, & Kveiborg M. (2015). The sorting protein PACS-2 promotes ErbB signalling by regulating recycling of the metalloproteinase ADAM17. Nature communications, 6, 7518.
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4

Mouse Liver Proteomic Analysis via Immunoblotting and IP

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Mouse livers were homogenized and subjects to immunoblotting and immunoprecipitation as described previously [21 (link)]. Whole-cell extracts from the livers and HeLa cells were homogenized and lysed in buffer containing 50 mM Tris-HCl (pH 7.5), 1% SDS, 5 mM EDTA, and 10 mM 2-ME, followed by sonication. The antibodies for α3, α6, β2, Rpt6, Rpn8, Rpn10 (N), Rpn10 (C), Rpn13, Uch37, mHR23B, Usp14, and polyubiquitin were described previously [21 (link), 59 (link)]. A polyclonal antibody that recognizes both ubiquilin-1 and ubiquilin-4 was raised by immunizing rabbits with recombinant full-length ubiquilin-4 proteins. For immunohistochemistry, monoclonal antibodies against Rpn13 were raised by immunizing rats with recombinant full-length Rpn13 proteins. The antibodies for Tubulin (sc-5286; Santa Cruz Biotechnology), Ki-67 (RM-9106; Thermo Scientific), Nrf1 (sc-13031; Santa Cruz Biotechnology), β-catenin (610153; BD biosciences), p62 (PM045; MBL), Actin (MAB1501R; Millipore), and GAPDH (MCA4739; AbD Serotec) were purchased. For immunoprecipitation, liver homogenates were immunoprecipitated with an anti-Rpt6 antibody as described previously [21 (link)]. Band intensities were quantified using Fusion software (M&S Instruments Inc.).
Hamazaki J., Hirayama S, & Murata S. (2015). Redundant Roles of Rpn10 and Rpn13 in Recognition of Ubiquitinated Proteins and Cellular Homeostasis. PLoS Genetics, 11(7), e1005401.
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5

PACS-2 Regulation of ADAM17-Mediated EGFR Signaling

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PMA and BB-94 were from Calbiochem. Geneticin, 1,10-phenanthroline monohydrate, MISSION Universal Negative Control siRNA #1, and anti-alkaline phosphatase monoclonal antibody (clone 8B6) were from Sigma-Aldrich. HALT Phosphatase Inhibitor Cocktail was from Thermo Scientific. Complete EDTA-free inhibitor cocktail was from Roche. Interferin transfection reagent was from PolyPlus, and siGENOME non-targeting siRNA pool #2, SMARTpool PACS-2 and ADAM17 siRNAs were from Dharmacon (Thermo Scientific). We additionally used PACS-2 siRNA from Qiagen and pooled three siRNAs (PACS2_6, PACS2_7 and PACS2_9). Recombinant murine TNF-α was from Strathmann Biotec AG. PACS-2 antibody (19508-1-AP) was from Proteintech. ADAM17 (ab39162), ADAM17 (ab2051), MT1-MMP (ab38971), ADAM10 (ab1997), and pEGFR (ab40815) antibodies were from Abcam. PACS-1 antibody 17703 and PACS-2 antibody 18193 were previously described53 (link),54 (link). Actin (MAB1501R) and EGFR (06–847) antibodies were from Millipore. ADAM9 (AF949), and ADAM17 (MAB9301) antibodies were from R&D Systems. PACS-2-HA expression plasmid was in a pcDNA.3 backbone40 (link) (Invitrogen), and green fluorescent protein (GFP) expression plasmid was from Clontech.
Dombernowsky S.L., Samsøe-Petersen J., Petersen C.H., Instrell R., Hedegaard A.M., Thomas L., Atkins K.M., Auclair S., Albrechtsen R., Mygind K.J., Fröhlich C., Howell M., Parker P., Thomas G, & Kveiborg M. (2015). The sorting protein PACS-2 promotes ErbB signalling by regulating recycling of the metalloproteinase ADAM17. Nature communications, 6, 7518.
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6

Quantification of CAMK2 Expression and Phosphorylation

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Two to three days after transfection, HEK cells were harvested and homogenized in lysis buffer (10 mM Tris‐HCl 6.8, 2.5% SDS, 2 mM EDTA), containing protease inhibitor cocktail (#P8340, Sigma), phosphatase inhibitor cocktail 2 (#P5726, Sigma) and phosphatase inhibitor cocktail 3 (#P0044, Sigma). Protein concentration in the samples was determined using the BCA protein assay kit (Pierce) and then lysate concentrations were adjusted to 1 mg/ml. Western blots were probed with primary antibodies against CAMK2G (C‐18; raised against the 478–495 C‐terminal peptide, 1:1000, sc‐1541, Santa Cruz; validated in this study by overexpression experiments), CAMK2A (6G9, 1:40.000, Abcam; validated in Elgersma et al. (2002)), CAMK2B (CB‐β1, 1:10.000, Invitrogen; validated in van Woerden et al. (2009)), Actin (MAB1501R, 1:20.000, Chemicon; validated in Antibodypedia (https://Antibodypedia.com), Ph‐Thr286/Thr287 (auto‐phosphorylated CAMK2 antibody; #06‐881; 1:1000; Upstate Cell Signaling Solutions; validated in Elgersma et al. (2002)) and RFP (#600401379, 1:2000, Rockland, validated in this study by overexpression experiments), and secondary antibodies (goat anti‐mouse (#926‐32210), goat anti‐rabbit (#926‐68021), and donkey anti‐goat (#926‐68074), all 1:15.000, LI‐COR). Blots were quantified using LI‐COR Odyssey Scanner and Odyssey 3.0 software.
Proietti Onori M., Koopal B., Everman D.B., Worthington J.D., Jones J.R., Ploeg M.A., Mientjes E., van Bon B.W., Kleefstra T., Schulman H., Kushner S.A., Küry S., Elgersma Y, & van Woerden G.M. (2018). The intellectual disability‐associated CAMK2G p.Arg292Pro mutation acts as a pathogenic gain‐of‐function. Human Mutation, 39(12), 2008-2024.
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7

Immunoblotting of Cell Signaling Proteins

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Immunoblotting was described previously [33 (link)]. The following primary antibodies were used: actin (MAB 150 1R, Chemicon), Cdk5 (AHZ0492, Life Technologies), NICD (4147 Cell Signalling), presenilin (5643, Cell Signaling).
Merk H., Zhang S., Lehr T., Müller C., Ulrich M., Bibb J.A., Adams R.H., Bracher F., Zahler S., Vollmar A.M, & Liebl J. (2016). Inhibition of endothelial Cdk5 reduces tumor growth by promoting non-productive angiogenesis. Oncotarget, 7(5), 6088-6104.
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8

MAP3K7 Signaling Pathway Analysis

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The cells were harvested in ice‐cold PBS, 48–72 h after transfection. Lysate samples were prepared by homogenizing the harvested HEK293Tcells in lysate buffer (10 mM Tris‐HCl 6.8, 2.5% SDS, 2 mM EDTA) containing protease inhibitor cocktail 2 (#P5726; Sigma) and 3 (#P0044; Sigma‐Aldrich) and protease inhibitor (#P8340; Sigma‐Aldrich). Protein concentrations were determined using the BCA kit (Pierce). Final working protein concentrations were adjusted to 1 mg/ml. Western blots were probed with primary antibodies against MAP3K7 (sc‐7967, 1:1000; Santa Cruz), phospho‐MAP3K7 (Thr187; #4536, 1:1000; Cell Signaling), extracellular signal‐regulated kinase (ERK)1/2 (#9102, 1:2000; Cell Signaling), phospho‐ERK1/2 (#9101, 1:2000; Cell Signaling), actin (MAB1501R, 1:20,000; Chemicon), RFP (#600401379, 1:2000; Rockland), nuclear factor‐κB (NFκB) (sc‐514451, 1:1000; Santa Cruz), phospho‐NFκB (sc‐136548, 1:1000, Santa Cruz), glyceraldehyde 3‐phosphate dehydrogenase (2118S, 1:2000; Cell Signaling), and TAB1 (67020‐1‐Ig, 1:10.000; Proteintech) and secondary antibodies (goat anti‐mouse [#926‐32210] and goat anti‐rabbit [#926‐68021], all 1:15,000, LI‐COR). Blots were quantified using LI‐COR Odyssey Scanner and Odyssey 3.0 software.
van Woerden G.M., Senden R., de Konink C., Trezza R.A., Baban A., Bassetti J.A., van Bever Y., Bird L.M., van Bon B.W., Brooks A.S., Guan Q., Klee E.W., Marcelis C., Rosado J.M., Schimmenti L.A., Shikany A.R., Terhal P.A., Nicole Weaver K., Wessels M.W., van Wieringen H., Hurst A.C., Gooch C.F., Steindl K., Joset P., Rauch A., Tartaglia M., Niceta M., Elgersma Y, & Demirdas S. (2022). The MAP3K7 gene: Further delineation of clinical characteristics and genotype/phenotype correlations. Human Mutation, 43(10), 1377-1395.
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9

Western Blot Analysis of Protein Targets

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The following antibodies were used at a dilution of 1:1000: actin (MAB1501R; Chemicon) and GR-α (3626–1; Epitomics). Secondary antibodies used were HRP-conjugated anti-mouse IgG (A9917; Sigma) and anti-rabbit IgG (A0545: Sigma). Dexamethasone (DN1187; BioBasic), Box 5 WNT5A antagonist (681673; Sigma), Human IgG antibody (orb27741; Biorbyt), ROR1 antibody (16540S; New England Biolabs), LGK-974(S7143; Selleckchem), Recombinant WNT5A (645-WN-010; Bio-techne).
Crozier M., Tubman J., Fifield B.A., Ferraiuolo R.M., Ritchie J., Zuccato K., Mailloux E., Sinha I., Hamm C, & Porter L.A. (2022). Frequently used antiemetic agent dexamethasone enhances the metastatic behaviour of select breast cancer cells. PLoS ONE, 17(9), e0274675.
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10

Quantitative Western Blot Analysis of CAMK2 Proteins

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2-3 days after transfection HEK cells were harvested and homogenized in lysis buffer (10mM Tris-HCl 6.8, 2.5% SDS, 2mM EDTA), containing protease inhibitor cocktail (#P8340, Sigma), phosphatase inhibitor cocktail 2 (#P5726, Sigma) and phosphatase inhibitor cocktail 3 (#P0044, Sigma). Protein concentration in the samples was determined using the BCA protein assay kit (Pierce) and then lysate concentrations were adjusted to 1 mg/ml. Western blots were probed with primary antibodies against CAMK2G (C-18; raised against the 478-495 C-terminal peptide, 1:1000, sc-1541, Santa Cruz; validated in this study by overexpression experiments), CAMK2A (6G9, 1:40.000, Abcam; validated in (Elgersma et al., 2002 (link))), CAMK2B (CB-β1, 1:10.000, Invitrogen; validated in (van Woerden et al., 2009 (link))), Actin (MAB1501R, 1:20.000, Chemicon; validated in Antibodypedia (http://Antibodypedia.com), Ph-Thr286/Thr287 (autophosphorylated CAMK2 antibody; #06-881; 1:1000; Upstate Cell Signaling Solutions; validated in (Elgersma et al., 2002 (link))) and RFP (#600401379, 1:2000, Rockland, validated in this study by overexpression experiments) and secondary antibodies (goat anti-mouse (#926-32210), goat anti-rabbit (#926-68021) and donkey anti-goat (#926-68074), all 1:15.000, LI-COR). Blots were quantified using LI-COR Odyssey Scanner and Odyssey 3.0 software.
Proietti Onori M., Koopal B., Everman D.B., Worthington J.D., Jones J.R., Ploeg M.A., Mientjes E., van Bon B.W., Kleefstra T., Schulman H., Kushner S.A., Küry S., Elgersma Y, & van Woerden G.M. (2018). The intellectual disability‐associated CAMK2G p.Arg292Pro mutation acts as a pathogenic gain‐of‐function. Human Mutation, 39(12), 2008-2024.
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