Rabbit monoclonal igg

Manufactured by Cell Signaling Technology

Sourced in United States

Rabbit monoclonal IgG is an immunoglobulin G (IgG) antibody derived from rabbit B cells. It is used as a tool in various laboratory applications, such as immunoassays and protein detection.

Automatically generated - may contain errors

Lab products found in correlation

Amersham imager 600, by GE Healthcare (2 mentions) Amersham imager, by Cytiva (2 mentions) Hybond polyvinylidene difluoride transfer membranes, by GE Healthcare (1 mentions) Complete mini, by Roche (1 mentions) Ecl prime western blotting detection reagent, by GE Healthcare (1 mentions) Anti β actin antibody, by Merck Group (1 mentions) Hybond, by Cytiva (1 mentions) Goat anti rabbit igg h l, by Bio-Rad (1 mentions) Rabbit polyclonal igg, by Proteintech (1 mentions) Nupage 4 12 bis trigel, by Thermo Fisher Scientific (1 mentions) Supersignal west dura, by Thermo Fisher Scientific (1 mentions) Protease inhibitor mixture, by Santa Cruz Biotechnology (1 mentions) Bovine serum albumin (bsa), by R&D Systems (1 mentions) Mouse monoclonal igg, by Abcam (1 mentions) Triton x 100, by Merck Group (1 mentions) Alexa fluor 594 donkey anti mouse igg h l, by Thermo Fisher Scientific (1 mentions) Hoechst 33342, by Thermo Fisher Scientific (1 mentions) Alexa fluor 488 donkey anti goat igg h l, by Thermo Fisher Scientific (1 mentions) Mouse monoclonal igg, by Santa Cruz Biotechnology (1 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

IgG rabbit (9 citations) Monoclonal rabbit (3 citations) Rabbit anti-mouse monoclonal IgG (2 citations) Anti-human PDCD4 rabbit monoclonal IgG (2 citations) Anti-cleaved Casp-3 rabbit IgG monoclonal antibodies (2 citations)

7 protocols using rabbit monoclonal igg

STAT3 Activation in GCIY Cells by IL-6 and TDMs

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GCIY was co-cultured with TDMs (ratio of TDMs/GCIY: 0, 2, 5, 10) or cultured in medium containing recombinant human IL-6 at a range of 0–100 ng/ml for 48 hours. Cells were washed with cold PBS and lysed with the SDS buffer containing protease inhibitors (cOmplete Mini, Roche Diagnostics GmbH, #11836153001). Equivalent amounts of protein from whole-cell lysates were loaded into each lane of 10% SDS–polyacrylamide gel and electrophoretically transferred to Hybond-polyvinylidene difluoride transfer membranes (GE Healthcare UK Ltd.). Membranes were incubated with the following primary antibodies overnight at 4°C: anti-signal transducer and activator of transcription 3 (STAT3; rabbit monoclonal IgG, diluted 1:1000; Cell Signaling Technology, # 14801, RRID:AB_2798618) and anti-phosphorylated STAT 3 (p-STAT3; rabbit monoclonal IgG, diluted 1:2000; Cell Signaling Technology, #9145, RRID:AB_2491009). Equal loading of samples was confirmed by probing with anti–β-actin antibody (Sigma-Aldrich, #A5441). Membranes were subsequently incubated with secondary antibodies for 1 hour. Peroxidase activity of secondary antibodies was detected using an ECL prime Western Blotting Detection Reagent (GE Healthcare UK Ltd., #RPN2232) and visualized using an Amersham Imager 600 (GE Healthcare UK Ltd.) according to the manufacturer’s protocol.

Sakamoto S., Kagawa S., Kuwada K., Ito A., Kajioka H., Kakiuchi Y., Watanabe M., Kagawa T., Yoshida R., Kikuchi S., Kuroda S., Tazawa H, & Fujiwara T. (2019). Intraperitoneal cancer-immune microenvironment promotes peritoneal dissemination of gastric cancer. Oncoimmunology, 8(12), e1671760.

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Western Blot Analysis of SQSTM1/p62 and OFD1

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Proteins were separated on 12.5% SDS-PAGE and then transferred to a PVDF membrane. The membrane was blocked with 5% milk in PBST for 1 h at room temperature and then incubated with the following primary antibodies: anti-SQSTM1/p62antibody (rabbit polyclonal IgG, Proteintech, Ca#18420, 1:1,000), anti-OFD1 antibody (rabbit polyclonal IgG, Proteintech, Ca#22851, 1:1,000) and anti-β-actin antibody (rabbit monoclonal IgG, Cell Signaling, Ca#4970, 1:1,000). Goat anti-rabbit IgG(H+L) (BIORAD Ca#1708241, 1:5,000) was used as the secondary antibody. The results were analyzed with an Amersham Imager 600 (GE Healthcare). We used β-actin as the index of the loaded protein content in each sample.

Kojima R., Hassan E., Ozawa F., Yamada-Namikawa C., Ogawa S., Mase S., Goto S., Nishikawa R., Inagaki H., Kato Y, & Sugiura-Ogasawara M. (2022). Abnormal accumulation of OFD1 in endometrial cancer with poor prognosis inhibits ciliogenesis. Oncology Letters, 24(1), 214.

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Measuring Phospho-NF-κB p65 in Lung Tissue

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Lungs were homogenized in radioimmunoprecipitation assay buffer, containing PMSF, natrium orthovanadate, phosphatase inhibitor mixture B, and protease inhibitor mixture (Santa Cruz Biotechnology, Santa Cruz, CA) on ice for 15 min and centrifuged at 17,000 × g at 4°C for 15 min to remove the cell debris. The amount of proteins was quantified by Quick Start Bradford Protein Assay (Bio-Rad Lab GmbH, Munich, Germany). For all samples, 50 μg protein was loaded in NuPAGE 4–12% Bis-Trigel (Invitrogen AG, Carlsbad, CA) and transferred to nitrocellulose membrane. The membrane was blocked with 5% milk powder and incubated with a primary Ab against phospho–NF-κB p65 (1:500, rabbit monoclonal IgG; Cell Signaling, Danvers, MA) overnight. Afterward we used HRP-conjugated secondary Abs against rabbit IgG (Cell Signaling) for 1 h. Primary Ab was visualized and enhanced by chemiluminescence with SuperSignal West Dura (Thermo Scientific, Rockford, IL). The amount of mouse β-actin detected by monoclonal anti-actin Ab clone C4 served as loading control (MP Biomedicals LLC, Solon, OH). The densitometric analysis was performed using ImageJ.

Baudiß K., de Paula Vieira R., Cicko S., Ayata K., Hossfeld M., Ehrat N., Gómez-Muñoz A., Eltzschig H.K, & Idzko M. (2016). C1P Attenuates Lipopolysaccharide-Induced Acute Lung Injury by Preventing NF-κB Activation in Neutrophils. Journal of immunology (Baltimore, Md. : 1950), 196(5), 2319-2326.

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Immunofluorescent Staining of Endoderm and Ectoderm

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Definitive endoderm was fixed with 4% paraformaldehyde (Sigma-Aldrich), permeabilized with 0.1% Triton X-100 (Sigma-Aldrich) and blocked with 3% BSA (Sigma-Aldrich). Primary antibodies were diluted in 1.5% BSA at a final concentration of 2 μg/μL for SOX17 (Goat Polyclonal IgG; R&D Systems, Cat# AF1924) and 1 μg/μL for OCT-3/4 (Mouse Monoclonal IgG, Santa Cruz Biotechnology, Cat# SC-5279) and incubated overnight. Donkey anti-Goat IgG (H + L) Alexa Fluor 488 (Thermo Fischer Scientific, Cat# A-11055) and donkey anti-mouse IgG (H + L) Alexa Fluor 594 (Thermo Fischer Scientific, Cat# R37115) were used as secondary antibodies. Ectoderm cells were fixed with 4% paraformaldehyde (Sigma-Aldrich), permeabilized with 100% methanol (Sigma-Aldrich), and blocked with 10% fetal bovine serum (Thermo Fischer Scientific). Primary antibodies were diluted in the blocking solution in a final concentration of 2 μg/μL and 1 μg/μL for PAX6 (Mouse Monoclonal IgG, Abcam, Cat# ab78545) and OCT3A (Rabbit Monoclonal IgG, Cell Signaling, Cat# C30A3), respectively, and incubated overnight. Donkey anti-rabbit (H + L) Alexa Fluor 488 (Thermo Fisher Scientific) and donkey anti-mouse (H + L) Alexa Fluor 594 (Thermo Fisher Scientific) were used as secondary antibodies. For both endoderm and ectoderm, nuclear staining was performed with Hoechst 33342 (Thermo Fischer Scientific).

Zambelli F., Mertens J., Dziedzicka D., Sterckx J., Markouli C., Keller A., Tropel P., Jung L., Viville S., Van de Velde H., Geens M., Seneca S., Sermon K, & Spits C. (2018). Random Mutagenesis, Clonal Events, and Embryonic or Somatic Origin Determine the mtDNA Variant Type and Load in Human Pluripotent Stem Cells. Stem Cell Reports, 11(1), 102-114.

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Transcription Factor Binding in ChIP

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Rabbit monoclonal anti-IRF-1 antibody (1:500), anti-CEBPA (1:300), rabbit monoclonal anti- cMyc antibody (1:500), anti-GATA1 antibody (1:200) and anti-AP1 (1:500) were used in ChIP assays with a rabbit monoclonal IgG (1:500; Cell signaling) as a negative control. The presence of predicted transcription factor binding regions pulled by this corresponding antibody was assessed by PCR. A small amount of pre-cleared DNA (before addition of antibodies) was set as an input control.

Yu H., Ding J., Zhu H., Jing Y., Zhou H., Tian H., Tang K., Wang G, & Wang X. (2020). LOXL1 confers antiapoptosis and promotes gliomagenesis through stabilizing BAG2. Cell Death and Differentiation, 27(11), 3021-3036.

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Quantification of IGF1R Signaling

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We performed the BioRad DC protein assay according to the manufacturer’s protocol (Biorad, Hercules, CA). For immunoblot analysis, 30 μg of whole-cell lysates were separated on 4–20% SDS-polyacrylamide gels, transferred to 0.45um nitrocellulose membranes. Membranes were blocked in 5% BSA prior to primary antibody exposure (overnight at 4C). The primary antibodies were: Rabbit monoclonal IgG against IGF1R β subunit (D23H3) (dilution 1:1000), Rabbit monoclonal IgG against phospho-IGF1R β subunit (Tyr 1135/1136) (dilution 1:1000), and mouse monoclonal IgG against alpha-tubulin (DM1A) from Cell Signaling Technologies (Beverly, MA). Secondary antibodies (anti-mouse IgG and anti-rabbit IgG) conjugated with horse-radish peroxidase were obtained from BioRad (Hercules, CA). Detection of immune-labeled proteins was performed using a commercial chemiluminescent assay (ECL prime; Amersham, Buckinghamshire, UK). Visualization and quantitative measurements were performed on the BioRad ChemiDoc Touch Imaging System, and densitometry was performed using Image J software. All immunoblot data shown are representative of at least three independent experiments. Unpaired T-tests were used to compare densitometric analyses between wild type and variant IGF1R.

Cabrera-Salcedo C., Hawkes C.P., Tyzinski L., Andrew M., Labilloy G., Campos D., Feld A., Deodati A., Hwa V., Hirschhorn J.N., Grimberg A, & Dauber A. (2019). Targeted Searches of the Electronic Health Record and Genomics Identify an Etiology in Three Patients with Short Stature and High IGF-I Levels. Hormone research in paediatrics, 92(3), 186-195.

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Quantitative Analysis of Apoptotic Markers

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Left ventricular muscle (100 mg) was added to extraction buffer, homogenized and centrifuged. Supernatants were collected and total amount of protein was quantified by the Bradford method. Electrophoresis was performed in acrylamide gels and proteins were transferred to nitrocellulose membranes, which were incubated in 5% skimmed milk. Subsequently, membranes were incubated with primary antibodies for caspase-3 (rabbit monoclonal IgG, Cell Signaling Technology, MA, USA) and Bcl-2 (rabbit monoclonal IgG, Santa Cruz Biotechnology, Europe) for 12 hours, followed by incubation with secondary antibodies. Immunodetection was performed using chemiluminescence in an ImageQuant LAS camera imaging system (General Electrics). Images were analyzed by Gel-Pro 32 (Media Cybernetics Rockville, USA). GAPDH (mouse monoclonal IgG, Santa Cruz Biotechnology, Europe) was used to normalize all proteins.

Mathias L.M.B.S., Alegre P.H.C., Dos Santos I.O.F., Bachiega T., Figueiredo A.M., Chiuso-Minicucci F., Fernandes A.A., Bazan S.G.Z., Minicucci M.F., Azevedo P.S., Okoshi M.P., Zornoff L.A.M., Paiva S.A.R, & Polegato B.F. (2019). Euterpe oleracea Mart. (Açai) Supplementation Attenuates Acute Doxorubicin-Induced Cardiotoxicity in Rats. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 53(2).

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