Rabbit anti mouse igg

Manufactured by Cell Signaling Technology

Sourced in United States

Rabbit anti-mouse IgG is a secondary antibody used in immunoassays to detect the presence of mouse immunoglobulin G (IgG). It is produced by immunizing rabbits with mouse IgG, and the resulting antibodies are purified from the rabbit serum. This product can be used to amplify the signal in various immunodetection techniques, such as Western blotting, ELISA, and immunohistochemistry, where the primary antibody is a mouse IgG.

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Lab products found in correlation

Goat anti rabbit igg, by Cell Signaling Technology (3 mentions) Pvdf membrane, by Merck Group (2 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (2 mentions) Laemmli buffer, by Bio-Rad (2 mentions) Cleaved caspase 3, by Cell Signaling Technology (2 mentions) Bcl xl, by Cell Signaling Technology (2 mentions) Bcl 2, by Cell Signaling Technology (2 mentions) Bicinchoninic acid kit, by Beyotime (1 mentions) Anti sgk1, by Cell Signaling Technology (1 mentions) Ab83905, by Abcam (1 mentions) Anti gapdh sc 32233, by Santa Cruz Biotechnology (1 mentions) Radioimmunoprecipitation assay lysis buffer, by Beyotime (1 mentions) Bicinchoninic acid protein assay kit, by Wuhan Boster Biological Technology (1 mentions) Hrp conjugated goat anti rabbit igg, by Cell Signaling Technology (1 mentions) Signalboost immunoreaction enhancer kit, by Merck Group (1 mentions) Rhodamine phalloidin, by Thermo Fisher Scientific (1 mentions) Nocodazole, by Merck Group (1 mentions) Taxol, by Merck Group (1 mentions) Rabbit anti cofilin, by Abcam (1 mentions) Mouse anti actin, by Merck Group (1 mentions)

Close spelling variants of this product

IgG rabbit (9 citations) Rabbit anti-IgG (8 citations) IgG (Mouse) (3 citations) Horseradish peroxidase (HRP)-conjugated donkey anti-rabbit and anti-mouse IgGs (2 citations)

21 protocols using rabbit anti mouse igg

Protein Extraction and Western Blot Analysis

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Cells were washed with cold PBS. Proteins were extracted with lysis buffer supplemented with a proteinase inhibitor. Cell lysates were centrifuged at 12,000 × g for 10 min at room temperature. Supernatants were collected and protein concentrations were quantified using a bicinchoninic acid kit (P0010S; Beyotime Institute of Technology). Then, proteins (35 mg) with loading buffer were resolved by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Western blots were developed using anti-ZIP4 (orb395779; Biorbyt, Cambridge, UK), anti-GAPDH (sc-32,233; Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti-GJA1 (ab51067; Abcam, Cambridge, UK), anti-SGK1 (12,103; Cell Signaling Technology, Danvers, MA, USA), anti-MET (ab51067; Abcam), anti-VEGFC (ab83905; Abcam), mouse anti-rabbit IgG (7074; Cell Signaling Technology) and rabbit anti-mouse IgG (7076; Cell Signaling Technology).

Li M., Fan K., Zheng B., Zekria D., Suo T., Liu H., Shen S., Liu H, & Ni X. (2021). Knockdown of SLC39A4 Expression Inhibits the Proliferation and Motility of Gallbladder Cancer Cells and Tumor Formation in Nude Mice. Cancer Management and Research, 13, 2235-2246.

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Western Blot Analysis of TRPM7 Protein Levels

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ASMCs were lysed with radioimmunoprecipitation assay lysis buffer (Beyotime Institute of Biotechnology, Shanghai, China). The extracts were collected and protein concentrations were measured using a bicinchoninic acid protein assay kit (Wuhan Boster Biological Technology, Ltd.). Equal quantities (40 μg) of protein were separated by 10% sodium dodecyl sulphate-polyacrylamide gel electrophoresis (Wuhan Boster Biological Technology, Ltd.) and blotted onto polyvinylidene fluoride (PVDF) membrane (Merck Millipore, Bedford, MA, USA). The PVDF membrane was blocked for nonspecific protein binding with Tris-buffered saline/Tween-20 (TBST; Guangzhou Whiga Technology Co., Ltd.) and 5% non-fat milk (Guangzhou Whiga Technology Co., Ltd.) at room temperature for 2 h. Then, the membrane was incubated overnight at 4°C with primary goat anti-TRPM7 (1:500; Abcam, Cambridge, UK) and primary mouse anti-β-actin (1:1,000; Sigma-Aldrich, St. Louis, MO, USA) monoclonal antibodies. Next, the membranes were washed with TBST, incubated with HRP-conjugated rabbit anti-goat IgG (1:500) and rabbit anti-mouse IgG (1:1,000) secondary antibodies (Cell Signaling Technology, Inc.) for 1 h, and then washed three times with TBST. The proteins were detected using an enhanced chemiluminescence system (a SignalBoost™ Immunoreaction Enhancer kit; Merck Millipore).

LIN X., YANG C., HUANG L., CHEN M., SHI J., OUYANG L., TANG T., ZHANG W., LI Y., LIANG R, & JIANG S. (2016). Upregulation of TRPM7 augments cell proliferation and interleukin-8 release in airway smooth muscle cells of rats exposed to cigarette smoke. Molecular Medicine Reports, 13(6), 4995-5004.

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Antibody-Based Cytoskeletal Analysis

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The following primary and secondary antibodies were used in this study. Rabbit anti-cofilin, rabbit anti-acetylated lysine, rabbit anti-flag, rabbit anti-CTTN, rabbit anti-phospho CTTN (Tyr421), rabbit anti-mouse IgG, (Cell Signaling), Rabbit anti-cofilin (Santa Cruz), Rabbit anti-cofilin, rabbit anti-phosphoSer3cofilin, rabbit-anti EB1, mouse anti-alpha tubulin (Abcam), mouse anti actin (Millipore), goat anti-mouse and anti-rabbit IgG HRP conjugate (Promega) and mouse TrueBlot Ultra Ig HRP (eBioscience). Rhodamine phalloidin was from Invitrogen. Reagents used include nocodazole, taxol (Sigma), trichostatin A (TSA; Calbiochem) and tubacin (provided by Ralph Mazitschek and Stuart Schreiber). Minimum essential medium-alpha modification (α-MEM), Dulbecco’s modified Eagle’s medium (DMEM) and fetal bovine serum (FBS) were purchased from Invitrogen (Carlsbad, CA).

Zalli D., Neff L., Nagano K., Shin N.Y., Witke W., Gori F, & Baron R. (2016). The Actin-Binding Protein Cofilin and Its Interaction With Cortactin Are Required for Podosome Patterning in Osteoclasts and Bone Resorption In Vivo and In Vitro. Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, 31(9), 1701-1712.

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Immunoblotting Analysis of Lung Cancer Cell Lines

Cited 1 time

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Whole cell protein lysates of HCC827, HCC827-ERL-R, H1975 and ROC-Res-H1975 cells treated with CFM 4.16 (10 μM), Tel (25 μM) and sorafenib (5 μM) either alone or in combinations were prepared by using RIPA buffer (Cell Signaling, Danvers, MA, USA) according to previously described methods (36 (link)). Protein estimation was carried out by using the bicinchoninic acid (BCA) assay. Briefly, 40 μg protein was loaded into each well of a 10% SDS-PAGE gel (Mini-PROTEAN® TGX™ Precast Gels). Protein was transferred to a PVDF membrane (Bio-Rad Laboratories, Hercules, CA, USA) after electrophoresis. After transfer, membranes were blocked for 4-6 h using 3% bovine serum albumin in PBS containing 0.1% Tween-20 (PBST). Blots were then incubated with primary antibodies (1:1,000) overnight followed by washing thrice with PBST for 5 min each, and finally incubated with appropriate HRP-conjugated secondary antibodies [rabbit anti-mouse IgG (catalog number: 7076S; Cell Signaling Technology)]; goat anti-rabbit IgG (catalog number: 7074S; Cell Signaling Technology) for 1 h at room temperature. After washing with PBST again thrice for 5 min each, the blots were incubated with SuperSignal West Pico Chemiluminescent substrate and their images were captured using Chemidoc Instrument (Bio-Rad). The immunoblots were quantified by densitometry scanning using NIH ImageJ software.

SURAPANENI S.K., NOTTINGHAM E., MONDAL A., PATEL N., ARTHUR P., GEBEYEHU A., KALVALA A.K., RISHI A.K, & SINGH M. (2021). Telmisartan Facilitates the Anticancer Effects of CARP-1 Functional Mimetic and Sorafenib in Rociletinib Resistant Non-small Cell Lung Cancer. Anticancer research, 41(9), 4215-4228.

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PTEN protein expression analysis in CLL cells

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Twenty-four hours after miRNA transfection, transfected CLL cells were lysed in RIPA buffer containing protease inhibitors and protein was extracted. The protein concentration was assayed by BCA (Beyotime) and 25 μg of protein was separated on a 10% SDS-PAGE gel, transferred to PVDF membranes followed by incubating with a murine monoclonal antibody against PTEN (Cell Signaling Technology) at 1:1000 dilutions. The secondary antibody used was rabbit anti-mouse IgG (Cell Signaling Technology) at 1:1000 dilutions at room temperature. The blot was stripped and reprobed with an anti-β-actin antibody (Cell Signaling Technology) to confirm equal loading. Signals were observed with ECL detection reagent (Pierce).

Zou Z.J., Fan L., Wang L., Xu J., Zhang R., Tian T., Li J.Y, & Xu W. (2014). miR-26a and miR-214 down-regulate expression of the PTEN gene in chronic lymphocytic leukemia, but not PTEN mutation or promoter methylation. Oncotarget, 6(2), 1276-1285.

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Immunohistochemical Analysis of Apoptosis

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4T1 tumor cells were treated with different concentrations of c-di-GMP as indicated in the text, fixed in 10% neutral buffered formalin, and permeabilized with 0.1% Triton X100 for 30 min. Endogenous peroxidase activity was quenched using 3% hydrogen peroxide for 10 minutes, and blocked by 5% normal donkey serum and 2% BSA for 1hour. The cells were then stained by immunohistochemistry methods, using a primary antibody to active caspase-3 (rabbit anti-mouse IgG Cell Signaling, Billerica, MA) 1:50 dilution for 1hour at RT, followed by a secondary antibody conjugated with HRP for 1hour at RT (Invitrogen, Grand Island, NY), and then followed with diaminobenzidine as the final chromogen. All slides were briefly counterstained with hematoxylin.

Chandra D., Quispe-Tintaya W., Jahangir A., Asafu-Adjei D., Ramos I., Sintim H.O., Zhou J., Hayakawa Y., Karaolis D.K, & Gravekamp C. (2014). STING ligand c-di-GMP improves cancer vaccination against metastatic breast cancer. Cancer immunology research, 2(9), 901-910.

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Serotonin and SERT Quantification

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[³H] 5-HT (28.1 Ci/mmol) and [³H] Citalopram (85.6 Ci/mmol) were purchased from Perkin Elmer (Boston, MA, USA). Cell culture media, supplements and antibiotics were all purchased from Invitrogen Corporation (Carlsbad, CA, USA). Human and mouse recombinant IL6 were obtained from eBioscience (San Diego, CA, USA), Stattic and Escitalopram were supplied by Sigma (Sigma Aldrich, Vienna, Austria), Tocilizumab was obtained from Roche (Vienna, Austria). Primary antibodies used were anti-STAT3 (Cell Signaling, #9139, Boston, MA, USA), anti-phospho-STAT3 (Cell Signaling, #9145), anti-beta-Tubulin (AbFrontier, #LF-MA20056, Seoul, Korea), and anti-SERT (Santa Cruz Biotechnology Inc., # Sc-1458, Santa Cruz, CA, USA). Secondary antibodies used were goat anti-rabbit IgG (Cell Signaling, #7074), rabbit anti-goat IgG (Santa Cruz Biotechnology Inc., #Sc-2020) and rabbit anti-mouse IgG (Cell Signaling, #7076).

Kong E., Sucic S., Monje F.J., Reisinger S.N., Savalli G., Diao W., Khan D., Ronovsky M., Cabatic M., Koban F., Freissmuth M, & Pollak D.D. (2015). STAT3 controls IL6-dependent regulation of serotonin transporter function and depression-like behavior. Scientific Reports, 5, 9009.

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Western Blot Analysis of Ubap1 Protein

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Western blotting was performed using an enhanced chemiluminescence system. Immunoblots were obtained for total protein extracts of the brains of 7-month-old wild-type (N = 3) and heterozygous Ubap1^+/E176Efx23 knock-in mice (N = 3). Briefly, the proteins were harvested from brain tissue by homogenization in RIPA buffer with a protease inhibitor cocktail (Roche). Equal amounts of proteins were separated on 10% SDS–polyacrylamide gels and then electrotransferred onto polyvinylidene difluoride membranes. After blocking with 3% BSA in PBS, the membranes were incubated with a primary antibody. After washing with PBS-0.1% Tween 20, filters were probed with horseradish peroxidase-conjugated sheep anti-rabbit IgG or rabbit anti-mouse IgG (Cell Signaling; Beverly, MA, USA). Immunoreactivity was detected with an enhanced chemiluminescence system (Amersham Biosciences, Buckinghamshire, UK). The chemiluminescent signals were captured with a Fujifilm luminescent image LAS-4000 analyzer (Fujifilm, Tokyo, Japan). Two kinds of rabbit polyclonal anti-UBAP1 antibodies (Sigma-Aldrich, SAB1307218 and Invitrogen, PA5-49644) were used in this study.

Shimozono K., Nan H., Hata T., Saito K., Kim Y.J., Nagatomo H., Ohtsuka T., Koizumi S, & Takiyama Y. (2022). Ubap1 knock-in mice reproduced the phenotype of SPG80. Journal of Human Genetics, 67(12), 679-686.

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Protein Expression and Quantification

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Proteins (10 μg for the (pro)renin receptor ((P)RR) and ACE2, and 20 μg for AT 1 R, loaded in duplicate), were separated on a 4-12% Bis-Tris NuPAGE gel (Invitrogen) and transferred to a polyvinylidene fluoride membrane (Amersham Hybond P 0.2 μM pore-size, GE Healthcare, Parramatta, New South Wales, Australia). After blocking overnight at 4°C in 5% skim milk, 5% bovine serum albumin (BSA), membranes were incubated with a primary antibody against (P)RR (Abcam, Cambridge, UK; ab40790, 1:1000), ACE2 (ab15348; 1:1000), or AT 1 R (ab9391; 1:400) for 2 h. Blots were exposed to a goat anti-rabbit IgG (Millipore, Burlington, MA, USA; #12-348, 1:5000) for (P)RR and ACE2, and rabbit anti-mouse IgG (Cell Signaling Technology, Danvers, MA, USA; #7076, 1:3000) for AT 1 R, for 1 h. Proteins were detected using an Amersham ECL detection kit (GE Healthcare Life Science) and Amersham Imager 600. Blots were washed and re-probed for β-actin using a rabbit polyclonal anti-β-actin antibody (Abcam; ab8227, 1:5000). The ratio of the protein of interest to β-actin was averaged for duplicate lanes and differences between blots were corrected for using an internal control (a pooled placental sample).

Wang Y., Lumbers E.R., Arthurs A.L., Corbisier de Meaultsart C., Mathe A., Avery-Kiejda K.A., Roberts C.T., Pipkin F.B., Marques F.Z., Morris B.J, & Pringle K.G. (2018). Regulation of the human placental (pro)renin receptor-prorenin-angiotensin system by microRNAs. Molecular human reproduction, 24(9).

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Dissecting cGAS-STING Signaling Pathway

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dUTP was from Sigma, RNA polymerase III inhibitor (ML-60218) was from Merck Millipore, dNTP (Fermentas), type I IFNα were from PBL Biomedical Laboratories, CpG (Invitrogen), polyIC and peptidoglycan (from Staphylococcus aureus, InvivoGen), Taq Polymerase (BIOTAQ DNA polymerase, Bioline), Pfu (Agilent Technologies), cGAS siRNA (sc-95512), pol III RPC39 siRNA (sc-36292), pol III RPC62 siRNA (sc-76188) were from Santa Cruz Biotechnology, STING (antibody #3337), phospho-IRF-3 (Ser396) (4D4G, rabbit mAb #4947), IRF-3 (D6I4C, XP rabbit mAb #11904), β-catenin antibody (amino-terminal antigen, #9581), mouse anti-rabbit IgG (conformation specific, L27A9, mAb #3678), anti-rabbit IgG, HRP-linked (antibody #7074), cGAS (D1D3G, mAb#15102) antibodies were from Cell Signaling Technology. APOBEC3A antibody (SAB4500753) was from Sigma Aldrich. RIG-I (E-5, sc-376882), pol III RPC39 (C 39-2, sc-23913), pol III RPC62 (I-18, sc-69534) antibodies were from Santa Cruz Biotechnology, Inc. Anti-mouse IgG, (HRP-linked antibody #NA931V) was from GE Healthcare. Monoclonal anti-β-actin−peroxidase (antibody #A3854) was from Sigma Aldrich. Human IFNα (IgA, mba-hifnα-3), hIFNβ (IgG, mbg-hifnβ-3), hIFNγ (IgA, mba-hifnγ-3) and Mouse IgG2a (mbg2a-ctrlm) antibodies used as control were from InVivogen.

Suspène R., Mussil B., Laude H., Caval V., Berry N., Bouzidi M.S., Thiers V., Wain-Hobson S, & Vartanian J.P. (2017). Self-cytoplasmic DNA upregulates the mutator enzyme APOBEC3A leading to chromosomal DNA damage. Nucleic Acids Research, 45(6), 3231-3241.

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