Anti mouse igg a9044

Manufactured by Merck Group

Sourced in United States

Anti-mouse IgG (A9044) is a laboratory reagent produced by Merck Group. It is a purified antibody that specifically binds to mouse immunoglobulin G (IgG) antibodies. This reagent can be used in various immunological techniques, such as ELISA, Western blotting, and immunohistochemistry, to detect and quantify mouse IgG in samples.

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A9044 (103 citations) Anti-IgG mouse (5 citations) IgG mouse (3 citations) Anti-Mouse IgG—Peroxidase (A9044) (3 citations) HRP-conjugated anti-mouse IgG (A9044) (3 citations) Anti-Mouse IgG-Peroxidase antibody A9044 (2 citations) Anti-mouse IgG-HRP conjugate (A9044; (2 citations) Anti-Mouse-HRP (IgG-Peroxidase conjugate; A9044 (2 citations)

7 protocols using anti mouse igg a9044

Andrographolide Modulation of MAPK Pathway

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Andrographolide (98% purity; Merck Millipore, Darmstadt, Germany) was dissolved in dimethyl sulfoxide (DMSO) as a concentrated stock solution. Primary monoclonal antibodies against anti-Ras (DCABH-9932) were purchased from Upstate Biotechnology Inc. (Lake Placid, NY, USA); phospho-p44/42 ErK1/2 (Thr202/Tyr204; 9101) and p44/42 p44/42 MAPK (Erk1/2; 4695) were purchased from Cell Signaling Technology, Inc., (Beverly, MA, USA). Horseradish peroxidase (HRP)-conjugated anti-rabbit IgG (A0545) and anti-mouse IgG (A9044) monoclonal secondary antibodies, and isoflurane and luciferin were purchased from Sigma-Aldrich (Merck Millipore, Darmstadt, Germany).

Fu S.L., Chen C.A., Hung L.C., Lee M.S., Chiou W.Y., Lin H.Y., Su Y.C., Lee C.C, & Hung S.K. (2016). Preliminary results of a non-invasive method to measure tumor size and distribution in vivo. Experimental and Therapeutic Medicine, 12(6), 3614-3620.

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Protein Expression Analysis in Cells

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Cells and tissues (n = 6) were added to ice-cold RIPA-buffer (Sigma-Aldrich Chemie, Munich, Germany) containing 1 µg/mL leupeptin, 1 mmol/L phenylmethylsulfonyl fluoride, 5 mmol/L NaF, 1 mmol/L Na₃VO₄ and 1 mmol/L dithiothreitol and disrupted in a TissueLyzer (Qiagen, Hilden, Germany). Proteins (40 µg) were separated on 10% (w/v) sodium dodecyl sulfate polyacrylamide gels and transferred to polyvinylidene difluoride membranes (Whatman, Dassel, Germany). Membranes were blocked with PBS containing 0.5% (v/v) Tween 20, 5% (w/v) fat-free milk and 2% (w/v) bovine serum albumin. Protein bands were detected using the primary antibodies anti-SSTR2 [UMB1, ab134152] (Abcam, Cambridge, UK), anti-chromogranin A [C-20, sc1488] (Santa Cruz Biotechnology, Heidelberg, Germany), anti-ß-actin [A5316] (Sigma-Aldrich). The peroxidase-conjugated secondary antibodies anti-mouse IgG [A9044] and anti-rabbit IgG [A0545] were purchased from Sigma-Aldrich. Specific binding was detected using SuperSignal™ West Pico/Dura Substrate (Life Technologies, Carlsbad, CA, USA). Densitometric analysis was performed using the TL100 image analysis software (TotalLab, Newcastle upon Tyne, UK) and normalized to ß-actin.

Ullrich M., Bergmann R., Peitzsch M., Zenker E.F., Cartellieri M., Bachmann M., Ehrhart-Bornstein M., Block N.L., Schally A.V., Eisenhofer G., Bornstein S.R., Pietzsch J, & Ziegler C.G. (2016). Multimodal Somatostatin Receptor Theranostics Using [64Cu]Cu-/[177Lu]Lu-DOTA-(Tyr3)octreotate and AN-238 in a Mouse Pheochromocytoma Model. Theranostics, 6(5), 650-665.

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Cloning and Characterization of U2AF Proteins

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To construct the expression plasmids for U2AF65 and U2AF35, Flag-tagged primer sets were designed to amplify the coding region of individual genes, and the PCR products were inserted into pcDNA3.0 between the HindIII and BamHI sites. U2AF35-Del-UHM was made by PCR to delete amino acids 65 to 147 from the U2AF35 coding region. All other site-specific mutations, including those for the U2AF35 mutants S34Y, S34F, Q157R and Q157P, and the U2AF65 mutants R18W, M144I and L187V, were generated by a PCR-based method (KOD Plus, TOYOBO). Supplementary Table 2 lists the primers used to construct U2AF-expression plasmids described above, and Supplementary Table 3 lists the primers used to construct and analyze individual minigenes in transfected cells. All constructs were verified by DNA sequencing.
The following primary antibodies were used: anti-U2AF65 (U4758, Clone MC3, Sigma-Aldrich, 1:10,000), anti-U2AF35 (ab86305, Abcam, 1:2,000), anti–β-actin (A1978, Clone AC-15, Sigma-Aldrich, 1:20,000), anti-GAPDH (10494-1-AP Proteintech, 1:10,000) and anti-Flag (F1804, Clone M2, Sigma-Aldrich, 1:3,000). Primary antibodies were detected with horseradish peroxidase (HRP)-labeled secondary antibodies (anti-rabbit IgG, A8275, Sigma-Aldrich, 1:10,000; anti-mouse IgG, A9044, Sigma-Aldrich, 1:10,000) for western blotting.

Shao C., Yang B., Wu T., Huang J., Tang P., Zhou Y., Zhou J., Qiu J., Jiang L., Li H., Chen G., Sun H., Zhang Y., Denise A., Zhang D.E, & Fu X.D. (2014). Mechanisms for U2AF to define 3′ splice sites and regulate alternative splicing in the human genome. Nature structural & molecular biology, 21(11), 997-1005.

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Protein Expression and Phosphorylation Analysis

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Primary: rabbit polyclonal anti-CDK/2 (M2), cat no. sc-1632 Santa Cruz Biotechnologies; mouse monoclonal (9E10) anti-c-Myc, cat no. SC-40 Santa Cruz Biotechnologies; rabbit polyclonal anti-p-c-Myc (Thr58/Ser 62), cat no. Sc-8000R, Santa Cruz Biotechnologies; mouse monoclonal anti-SCML2 (SCMAD14a), cat no. ab51506 Abcam; rabbit polyclonal antip-Src (Tyr416), cat no. 2101S, Cell Signaling; rabbit polyclonal anti-Src antibody, cat no. 2108S, Cell Signaling, rabbit monoclonal anti-p27 Kip1 (D69C12) XP^® cat no. 3686; Santa Cruz Biotechnology; mouse monoclonal p21 (F-5), cat no. sc-6246, Santa Cruz Biotechnologies; mouse monoclonal anti Nanog, clone 7F7-1, cat no. MABD24, EMD Millipore; rabbit polyclonal anti-Bmi-1 antibody, cat no. ab38295, Abcam. Mouse monoclonal anti-tubulin, cat no. T5168, Sigma. Secondary: anti-mouse IgG (A9044; Sigma-Aldrich); and goat anti-rabbit IgG peroxidase conjugate (A0545; Sigma-Aldrich).

GALOIAN K., QURESHI A., D’IPPOLITO G., SCHILLER P.C., MOLINARI M., JOHNSTONE A.L., BROTHERS S.P., PAZ A.C, & TEMPLE H.T. (2015). Epigenetic regulation of embryonic stem cell marker miR302C in human chondrosarcoma as determinant of antiproliferative activity of proline-rich polypeptide 1. International Journal of Oncology, 47(2), 465-472.

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Chondrocytic Cell Culture and Transfection

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HEK 293T cells were cultured in Dulbecco’s modified Eagle’s medium (DMEM) supplemented with 10% fetal bovine serum (FBS; Hyclone, Logan, UT, U.S.A.) at 37°C under 5% CO₂. ATDC5 cells, a murine chondrocytic cell line, were cultured in DMEM/F12 medium (Hyclone) containing 1 mM phosphorus, 0.25 mM glycine, and 0.15 mM proline. In addition, the following reagents were used in the study: 2OD primers (Sangon Biotech, Shanghai, China); EcoRI and BglII restriction enzymes (Thermo Fisher Scientific, Waltham, MA, U.S.A.); T4 ligase (Thermo Fisher Scientific); DL-2000 DNA Marker (Thermo Fisher Scientific); high-glucose DMEM (Hyclone); trypsin (Hyclone); cycloheximide (CHX) (Sigma–Aldrich, St. Louis, MO, U.S.A.); anti-Myc (M4439), anti-Flag (F3165), anti-HA (H9658), anti-Col II (MAB8887), anti-heat shock protein (HSP)90 (SAB1305541) primary antibodies (Sigma–Aldrich); and anti- mouse IgG (A9044, Sigma–Aldrich).

Liu F., Fu Q., Li Y., Zhang K., Tang M., Jiang W., Bo B., Cui Y, & Kong L. (2019). USP21 modulates Goosecoid function through deubiquitination. Bioscience Reports, 39(7), BSR20182148.

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Culturing Human Keratinocyte Cell Line

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Human keratinocyte cell line HaCaT cells (American Type Culture Collection, Manassas, VA, USA) was grown in DMEM with 10% fetal bovine serum (FBS) and 1% antibiotics (penicillin/streptomycin) supplementation. The cultivated cells were maintained in a 37 °C incubator with a humidified 5% CO₂ environment.
Antibodies against AhR (sc-133088) and CYP1A1 (sc-25304) were obtained from Santa Cruz Biotechnology (Dallas, TX, USA). Antibodies against p-TRPV1 (Ser502) (PA5-64860) were obtained from Invitrogen (Carlsbad, CA, USA). Antibodies against β-actin (A5316), anti-rabbit immunoglobulin G (IgG) (A0545), and anti-mouse IgG (A9044) were obtained from Sigma-Aldrich (Sigma-Aldrich, St. Louis, MO, USA).

Choi S., Lee J.H., Oh S.W., Yu E., Kwon K., Jang S.J., Shin D.S., Moh S.H, & Lee J. (2023). Anti-Pollutant Activity of Porphyra yezoensis Water Extract and Its Active Compound, Porphyra 334, against Urban Particulate Matter-Induced Keratinocyte Cell Damage. Marine Drugs, 21(2), 121.

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Quantifying Arc/Arg3.1 Protein Levels

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Mice were decapitated after diethyl- ether anesthesia, and their brains were rapidly removed and frozen at −80 °C. Coronal brain sections (300 μm) were prepared using a cryostat (HM520; Thermo Fisher Scientific, Waltham, MA, USA). The basolateral amygdala (0.90 to 2.00 mm posterior to bregma) was punched out and homogenized in RIPA buffer (08714-04, Nacalai Tesque, Kyoto, Japan). Protein concentrations were normalized across homogenates using the BCA method (Thermo Scientific). Equal amounts of protein were electrophoresed on 5–20% SDS polyacrylamide gels and transferred to nitrocellulose membranes. Western blots were blocked in blocking buffer (03953-95, Nacalai Tesque, JAPAN) and then incubated with an anti-Arc/Arg3.1 antibody (sc-17839, Santa Cruz Biotechnology) at a 1:1000 dilution or with an anti-β-actin antibody (A3854, Sigma) at a 1:10,000 dilution. After incubation with anti-Mouse IgG (A9044, Sigma) at a 1:100,000 dilution, bands were developed with a chemiluminescent substrate (RPN2132, GE Healthcare). The immunopositive signals were quantified by ImageQuant LAS 4000 (GE Healthcare). Arc/Arg3.1 signals were normalized with β-actin signals.

Nakayama D., Hashikawa-Yamasaki Y., Ikegaya Y., Matsuki N, & Nomura H. (2016). Late Arc/Arg3.1 expression in the basolateral amygdala is essential for persistence of newly-acquired and reactivated contextual fear memories. Scientific Reports, 6, 21007.

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