Rabbit anti mouse igg

Manufactured by Merck Group

Sourced in United States

Rabbit anti-mouse IgG is a laboratory reagent used to detect the presence of mouse immunoglobulin G (IgG) in biological samples. It is a polyclonal antibody raised in rabbits that specifically binds to mouse IgG.

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Close spelling variants of this product

Anti-mouse and anti-rabbit IgGs (2 citations) Rabbit anti-IgG (9 citations) Anti-IgG mouse (5 citations) IgG rabbit (4 citations) IgG mouse (3 citations) Rabbit anti- (2 citations)

30 protocols using rabbit anti mouse igg

Influenza Virus Infection in BALB/c Mice

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Six-week-old female BALB/c mice (Beijing Experimental Animal Center, Beijing, China) were lightly anesthetized with CO₂ and inoculated i.n. with 10⁶ 50% egg infective doses (EID₅₀) of H3N2 avian influenza virus in a volume of 50 μL. Control mice were inoculated with 50 μL PBS. On day 3 post-inoculation (p.i.), three mice in each group were euthanized and their organs, including brains, nasal turbinates, spleens, kidneys and lungs, were collected for virus titration. The remaining five mice were monitored daily for weight loss and mortality for the following 2 weeks. The histological study of the lung sample was performed as described previously [9 (link)]. A monoclonal antibody against the NP protein of A/duck/Zhejiang/11/2000(H5N1) virus and rabbit anti-mouse IgG as the secondary antibody (Sigma-Aldrich) were used in the immunohistochemical (IHC) assays.

Guan L., Shi J., Kong X., Ma S., Zhang Y., Yin X., He X., Liu L., Suzuki Y., Li C., Deng G, & Chen H. (2019). H3N2 avian influenza viruses detected in live poultry markets in China bind to human-type receptors and transmit in guinea pigs and ferrets. Emerging Microbes & Infections, 8(1), 1280-1290.

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TNF-α Proteolysis by Karilysin

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Recombinant human TNF-α (1 μg) was incubated at 37°C with karilysin (10 ng - 10 μg) in 100 mM Tris- HCl and 5 mM CaCl₂, pH 8.0, at different E:S molar ratios ranging from 1:0.1 to 1:100. After 12h of incubation samples were separated on 12% polyacrylamide gel and stained with silver or electrotransferred onto nitrocellulose membranes (nitrocellulose BioRad) in buffer composed of 25 mM Tris, 0.2 M glycine, 20% methanol (30 V, overnight). Membranes were stained with Ponceau S to visualize the efficiency of transfer and confirm the loading precision (same amount of protein loaded per well). Non-specific binding sites were blocked with 3% BSA in TTBS buffer (20 mM Tris, 0.5 M NaCl, pH 7.5 with 0.05% Tween 20) for 1h, followed by 1-2h incubation with the relevant primary antibody: 100-fold diluted murine anti-human TNF-α or 10,000-fold diluted anti-β-actin (BD Transduction Lab.). Membranes were washed extensively in TTBS buffer and incubated with secondary horseradish peroxidase (HRP)-conjugated antibodies, 10,000-fold diluted rabbit anti-mouse IgG (Sigma), for 1h in TTBS buffer containing 1.5% BSA. Membranes were washed (4 × 15 min) in TTBS buffer and blots were developed using ECL detection (Western Blotting Detection Reagents; Amersham Biosciences).

Bryzek D., Ksiazek M., Bielecka E., Karim A.Y., Potempa B., Staniec D., Koziel J, & Potempa J. (2014). A pathogenic trace of Tannerella forsythia – shedding of soluble fully active tumor necrosis factor alpha from the macrophages surface by karilysin. Molecular oral microbiology, 29(6), 294-306.

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Comparative Protein Expression Analysis of TNBC Cells

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Total protein was isolated from cultured MDA MB 231, MDA MB 468, and MDAMB453 TNBC cells as well as from cultured MCF10A fibrocystic disease cells with the lysis buffer RIPA plus protease inhibitor cocktail. The homogenates were centrifuged at 17,000× g for 15 min at 4 °C. The supernatants were collected, and protein concentration was measured with the Bradford protein assay (Bio-Rad protein assay, Hercules, CA, USA). Thirty micrograms of protein samples were loaded each time into SDS-PAGE gels and transferred to nitrocellulose membranes (Whatman, Little Chalfont, UK) using the semi-dry transfer system (Bio-Rad). The membranes were blocked with 5% dry milk dissolved in Tris-buffered saline (1×) containing 0.1% Tween-20 for 1 h at room temperature (RT). The membranes were incubated with primary antibodies at 4 °C overnight followed by secondary antibodies for 1.30 h at RT. The primary antibodies in the Western blot were rabbit anti-EPHA2 (Santa Cruz, CA, USA, sc-924), mouse anti-EPHA4 (SantaCruz, sc-D-4), rabbit anti-EPHA7 (Santa Cruz, sc-1015), and mouse anti-beta actin (Sigma, A5441). The secondary antibodies were rabbit anti-mouse IgG (Sigma, A9044) (1:20,000 dilution) and goat anti-rabbit IgG (Sigma, A6154) (1:10,000 dilution).

Nikas I., Giaginis C., Petrouska K., Alexandrou P., Michail A., Sarantis P., Tsourouflis G., Danas E., Pergaris A., Politis P.K., Nakopoulou L, & Theocharis S. (2022). EPHA2, EPHA4, and EPHA7 Expression in Triple-Negative Breast Cancer. Diagnostics, 12(2), 366.

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Isolation and Enrichment of Nascent DNA

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Genomic DNA was isolated by incubating cells in SDS-PK buffer (0.5% (wt/vol) sodium dodecyl sulfate (SDS), 50 mM Tris-HCL, 0.01M EDTA, 1M NaCl and 0.2 mg/ml proteinase K) at 56 °C for 2 h. Phenol-chloroform extraction was performed and genomic DNA was precipitated in 1 volume of isopropanol at -20 °C. DNA was pelleted, washed with ethanol and resuspended in TE buffer. Genomic DNA was fragmented to an average size of 200 bp using a Branson Digital Sonifier (Model 250) and a Branson 101-148-063 microtip. DNA was sonicated using 40% amplitude for a total of 4 minutes. A double-antibody immunoprecipitation was performed to isolate nascent (BrdU labeled) strands of DNA. For each immunoprecipitation reaction, at least 120 ng of sonicated DNA was used. DNA was first heat denatured at 95 °C for 5 min and rapidly cooled on ice. 12.5 μg primary antibody (mouse anti-BrdU, BD Biosciences Pharmingen, cat. no. 555627) was added to the ssDNA suspension with constant rocking for 20 minutes followed by addition of 20 μg of secondary antibody (rabbit anti-mouse IgG, Sigma, cat. no. M-7023) for 20 min. Antibody-DNA complexes were then pelleted, resuspended and incubated in digestion buffer (50mM Tris-HCl, 0.01M EDTA, 0.5% SDS and 0.25 mg/ml proteinase K) at 37 °C overnight. Nascent ssDNA was subsequently purified by phenol-chloroform extraction and ethanol precipitation.

Charlton J., Downing T.L., Smith Z.D., Gu H., Clement K., Pop R., Akopian V., Klages S., Santos D.P., Tsankov A.M., Timmermann B., Ziller M.J., Kiskinis E., Gnirke A, & Meissner A. (2018). Global delay in nascent strand DNA methylation. Nature structural & molecular biology, 25(4), 327-332.

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Oleanolic Acid Modulates Glucose Metabolism

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Oleanolic acid (structure shown in Figure 1) was obtained from the Center for Drug Discovery at China Pharmaceutical University. Metformin (purity > 98%) was obtained from Sigma (St. Louis, MO, USA). The mouse insulin enzyme immunoassay ELISA kit was purchased from Invitrogen. Serum triglyceride (TG), total cholesterol (TC), high-density lipoprotein cholesterol (HDL-C), and low-density lipoprotein cholesterol (LDL-C) kits were purchased from Whitman Biotech (Nanjing, Ltd., China). Antibody (Ab) for G-6-Pase was purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA). TORC2 was from Millipore (Billerica, MA, USA), and phospho-CREB and β-actin were from Abcam (Cambridge, MA, USA). The Abs against protein kinase B (PKB/Akt), phospho-Ser473-Akt (pAkt), PI3K, phospho-PI3K, AMPK, phosphor-AMPK, ACC, phosphor-ACC, PEPCK1, mTOR, and phospho-mTOR were purchased from Cell Signaling Technology (Beverly, MA, USA). The HRP-conjugated secondary Abs, affinity-purified mouse anti-rabbit IgG, and rabbit anti-mouse IgG were purchased from Sigma (St. Louis, MO, USA).

Wang X., Chen Y., Abdelkader D., Hassan W., Sun H, & Liu J. (2015). Combination Therapy with Oleanolic Acid and Metformin as a Synergistic Treatment for Diabetes. Journal of Diabetes Research, 2015, 973287.

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Integrin Activation and Conformational Analysis

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HEK293T transfected with the αLβ2 integrin or its mutants were labeled with 0.5 mg/ml EZ-link Sulfo-NHS-LC-Biotin (Thermo Fisher Scientific) on cells surface. Labeled cells were collected and incubated with quadruplet conditions: mAb MHM23; mAb KIM127 with or without αLβ2 activator (Mg/EGTA: 5 mM MgCl₂ plus 1.5 mM EGTA); and irrelevant mAb LPM19c for 30 min at 37 °C. After that, cells were washed and lysed in lysis buffer (10 mM Tris, 150 mM NaCl, 0.15 mM CaCl₂, 0.5 mM MgCl₂, 1% (v/v) Nonidet P-40, pH 8.0) for 20 min on ice. Cell lysates were incubated with 25% protein-A Sepharose (GE healthcare) beads which were pre-coated with rabbit anti-mouse IgG (Sigma) for 3 h at 4 °C. Beads were washed for 3 times. Bound proteins were eluted and loaded on SDS acrylamide gel under reducing condition before electroblotting onto PVDF membrane. Blot was incubated with streptavidin conjugated HRP (GE healthcare) at RT for 1 h followed by ECL detection method.

Guan S., Tan S.M., Li Y., Torres J, & Alex Law S.K. (2016). Function and conformation analyses of an aspartate substitution of the invariant glycine in the integrin βI domain α1-α1′ helix. Biochemistry and Biophysics Reports, 7, 214-217.

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Antibody Response to Recombinant Proteins

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Purified recombinant proteins, PSMC5 (TP301251), MYPT1 (TP323540) and TFRC (TP300980) expressed in human HEK293 cells were purchased from Origene. One microgram of purified protein was denatured by boiling in SDS-PAGE sample buffer and resolved on a NuPAGE 4-12% Bis-Tris gel (Invitrogen). Proteins in the gel were transferred onto nitrocellulose membrane using a semi-dry apparatus (Invitrogen). The membrane was cut into individual lanes and was blocked in 5% bovine serum albumin (BSA, Invitrogen) in 0.1% Tween 20-PBS (PBS-T) buffer for 1 hour at room temperature. After blocking, each individual lane was probed with either pre-vaccination or post-vaccination serum at 1:1000 dilution. A lane was used as a control and probed with mouse anti-FLAG antibody overnight at 4°C. The membrane was incubated with the peroxidase-conjugated secondary antibodies, goat anti-human IgG antibody (Sigma, A8419) for patient serum lanes or rabbit anti-mouse IgG (Sigma, A9044) for control lane. ECL Western Blotting Detection Reagents (GE Healthcare) was used for 1 minute at room temperature for developing. Chi squared analysis was used to test for statistical significance.

Jhaveri D.T., Kim M.S., Thompson E.D., Huang L., Sharma R., Klein A.P., Zheng L., Le D.T., Laheru D.A., Pandey A., Jaffee E.M, & Anders R.A. (2016). Using Quantitative Seroproteomics to Identify Antibody Biomarkers in Pancreatic Cancer. Cancer immunology research, 4(3), 225-233.

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Nitrocellulose-based Immunochromatographic Assay Development

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Immobilizations of the antigen (TM CYA) and the antibody control (rabbit anti-mouse IgG, Sigma) onto nitrocellulose membrane were performed by the passive physical adsorption in the line pattern. The BioDot^®7x100^TM (BioDot, Irvine, CA) dispensing platform was utilized for this purpose. The transferring of protein solution was performed by using a micro-syringe pump dispenser. The rate of transfer was 1 μl/cm. A 1.25 cm of nitrocellulose membrane (AE98 Fast; Whatman Schleicher & Schuell) was sprayed at the test line with TM CYA (> 50 kDa protein after diafiltration in 5 mM Tris-HCl pH 8.5) and rabbit anti-mouse IgG (1 mg/ml in 1x PBS pH 7.4) at the control line. The lined nitrocellulose membrane was immediately placed in a dehumidifier cabinet for 30 min. Subsequently, the non-lined surface of the nitrocellulose membrane was blocked by submersion in the blocking reagent (0.5% w/v of casein, 0.2% w/v of trehalose dissolved in 2 mM Na₂B₄O₇ pH 9.0). The submersed nitrocellulose membranes were then placed on tissue papers and dried in a dehumidifier cabinet for 30 min. The blocked nitrocellulose membranes were stored at room temperature for 18–24 hr. before being assembled into the ICT strip system.

Pruksaphon K., Intaramat A., Ratanabanangkoon K., Nosanchuk J.D., Vanittanakom N, & Youngchim S. (2018). Development and characterization of an immunochromatographic test for the rapid diagnosis of Talaromyces (Penicillium) marneffei. PLoS ONE, 13(4), e0195596.

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Quantification of Anti-AChR Antibodies

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Sera from each mouse were prepared from bleeding collected 3 weeks after the secondary immunization. The concentration of Abs reactive to mouse AChR was determined in individual sera by RIA, as previously described (29 (link)). Briefly, mouse AChR was extracted from leg muscles and labeled with 2 × 10⁻⁹ M ¹²⁵I-labeled α-bungarotoxin (Amersham). A dilution range of serum samples was incubated overnight with 200 μl of labeled mouse AChR. Antibody-AChR complexes were captured by adding an excess of rabbit anti-mouse IgG (Sigma-Aldrich). The radioactivity of the complexes was measured in a gamma counter. Values of ¹²⁵I-labeled α-bungarotoxin-AChR pelleted in the presence of normal mouse serum were subtracted from the assay values. Corrections for inter-assay variability were made based on serial dilutions of an EAMG standard control serum pool tested in each assay. The antibody titers were expressed as moles of ¹²⁵I-labeled α-bungarotoxin binding sites precipitated per liter of serum.

Bernard I., Sacquin A., Kassem S., Benamar M., Colacios C., Gador M., Pérals C., Fazilleau N, & Saoudi A. (2018). A Natural Variant of the Signaling Molecule Vav1 Enhances Susceptibility to Myasthenia Gravis and Influences the T Cell Receptor Repertoire. Frontiers in Immunology, 9, 2399.

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NSCLC Cell Line Culture and Pioglitazone Treatment

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The human NSCLC H1299, H460, A549, H1975, HCC827 and human bronchial epithelial Beas2B cell lines were provided by American Type Culture Collection (ATCC, Manassas, VA, USA) and maintained in RPMI 1640 (Sigma-Aldrich) medium supplemented with 10% fetal bovine serum (FBS; Life Technologies, Gaithersburg, MD) in a humidified atmosphere with 5% CO₂. The identity of all cell lines was confirmed by STR profiling (Promega) on an ad hoc basis prior to performing experiments and repeated after the majority of the experiments were performed.
Pioglitazone was purchased from Sigma-Aldrich.Forin vitro studies, Pioglitazone was dissolved in sterile dimethylsulfoxide (DMSO) and the stock solution (10 mM) was stored in aliquots at − 20 °C. Working concentrations were diluted in culture medium just before each experiment.
Primary antibodies for western blot analysis against were obtained from Cell Signaling Technology; the following secondary antibodies from Bio-Rad were used: goat anti-rabbit IgG, rabbit anti-mouse IgG and monoclonal anti-α-tubulin antibody (T8203) from Sigma Chemical Co.

Ciaramella V., Sasso F.C., Di Liello R., Corte C.M., Barra G., Viscardi G., Esposito G., Sparano F., Troiani T., Martinelli E., Orditura M., De Vita F., Ciardiello F, & Morgillo F. (2019). Activity and molecular targets of pioglitazone via blockade of proliferation, invasiveness and bioenergetics in human NSCLC. Journal of Experimental & Clinical Cancer Research : CR, 38, 178.

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