Anti mouse or anti rabbit igg

Manufactured by GE Healthcare

Sourced in United States

Anti-mouse or anti-rabbit IgG is a laboratory reagent used in various immunoassays and other techniques. It is designed to specifically bind to mouse or rabbit immunoglobulin G (IgG) antibodies, respectively. This reagent can be used to detect, capture, or quantify target proteins or other analytes in biological samples.

Automatically generated - may contain errors

Lab products found in correlation

Pierce bca, by Thermo Fisher Scientific (1 mentions) Quantity one software, by Bio-Rad (1 mentions) Anti tubulin, by Merck Group (1 mentions) Anti creb, by Merck Group (1 mentions) Gel doc 2000 imaging system, by Bio-Rad (1 mentions) Phospho creb, by Merck Group (1 mentions) Cell extraction buffer, by Thermo Fisher Scientific (1 mentions) Notch1, by Cell Signaling Technology (1 mentions) Glut1, by Cell Signaling Technology (1 mentions) Tead1, by Santa Cruz Biotechnology (1 mentions) Jagged1, by Santa Cruz Biotechnology (1 mentions) Pepck, by Cell Signaling Technology (1 mentions) β actin, by Cell Signaling Technology (1 mentions) Amersham enhanced chemiluminescence, by GE Healthcare (1 mentions) Glut3, by Cell Signaling Technology (1 mentions) P taz ser89, by Cell Signaling Technology (1 mentions) Aldoa, by Cell Signaling Technology (1 mentions) Luminescent image analyzer las 4000 system, by Fujifilm (1 mentions) Mini protean tetra cell, by Bio-Rad (1 mentions) Immun star westernc chemiluminescence kit, by Bio-Rad (1 mentions)

6 protocols using anti mouse or anti rabbit igg

Nuclear Protein Extraction and Western Blot

Check if the same lab product or an alternative is used in the 5 most similar protocols

Nuclear extracts of mouse PF cortex were prepared in 0.25 M sucrose buffer (sucrose 0.25 M, Tris 50 mM, EDTA 1 mM, imidazole 3 mM, pH 7.0 + proteases inhibitor cocktail). Samples were centrifuged 10 min at 250 g and nuclear fraction was resuspended in Laemmli buffer. All samples were sonicated before protein assay (BCA Pierce, Thermoscientific) and Western blotting was performed on 20 µg of protein lysates. Membranes were incubated overnight at 4°C with the primary antibodies; anti-HDAC2 1∶1500 (Abcam), anti-H3 1∶10000 (Millipore), anti-tubulin 1∶4000 (Sigma), anti-CREB and phospho-CREB 1∶1000 (Millipore). Washes with PBS-Tween (0.005%) were followed by incubation with secondary antibody (1∶10 000 anti-mouse or anti-rabbit IgG) (GE Healthcare) coupled to horseradish peroxidase and revealed by ECL. For quantification, the membranes were stripped and reincubated with an anti-tubulin or an anti-H3 antibody. Immunoreactive bands were quantified with an electrophoresis Gel Doc 2000 imaging system coupled to a Quantity one software (Bio-Rad).

Hendrickx A., Pierrot N., Tasiaux B., Schakman O., Kienlen-Campard P., De Smet C, & Octave J.N. (2014). Epigenetic Regulations of Immediate Early Genes Expression Involved in Memory Formation by the Amyloid Precursor Protein of Alzheimer Disease. PLoS ONE, 9(6), e99467.

+ Open protocol

+ Expand

Western Blot Analysis of Cellular Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols

Total protein was isolated from cells using Cell Extraction Buffer (Biosource, Camarillo, CA) supplemented with protease and phosphatase inhibitors and precleared using centrifugation, followed by measuring protein concentrations using the BCA Protein Assay kit (Pierce, Rockford, IL). The primary antibodies including TAZ, CTGF, Notch1, Hes1, LDHA, PFKB3, PEPCK, PKM2, PGK1, HK2, GLUT1, GLUT3, ALDOA, p-TAZ (Ser89), and β-actin were purchased from Cell Signaling Technology (CA, US). Jagged1 and TEAD1 were purchased from Santa Cruz Biotechnology (CA, US). Appropriate secondary antibodies conjugated to horseradish peroxidase were used, including anti-mouse or anti-rabbit IgG (GE-Healthcare, CA, US). Proteins were visualized by Amersham enhanced chemiluminescence (GE-Healthcare, CA, US). Immunohistochemistry assay was performed as previously described [7 (link)].

Xie M., Fu X.G, & Jiang K. (2021). Notch1/TAZ axis promotes aerobic glycolysis and immune escape in lung cancer. Cell Death & Disease, 12(9), 832.

+ Open protocol

+ Expand

Immunoblot Analysis of SSAO Protein

Check if the same lab product or an alternative is used in the 5 most similar protocols

Tissue homogenates (10 μg) were denatured in loading buffer (Laemmli Sample Buffer, BioRad) for 5 min at 95°C and loaded on an acrylamide SDS/PAGE gel (Bio-Rad) in a Mini-PROTEAN Tetra Cell (Bio-Rad). Resolved protein was subsequently transferred to a nitrocellulose membrane (Bio-Rad) with a Mini Trans-Blot Module. The membranes were blocked for 1 h at room temperature (RT) in 0.1% Tween 20 in TBS buffer (10 mM Tris-Base and 15 mM NaCl, pH 7.5) containing 5% nonfat dry milk and incubated with primary antibodies (rabbit anti-SSAO, clone H43, and anti β-actin, Santa Cruz Biotechnology, Dallas, TX, USA) in blocking solution. After several washes, the membrane was incubated with an appropriate horseradish peroxidase- (HRP-) coupled secondary antibody (anti-mouse or anti-rabbit IgG, GE Healthcare, Chicago, IL, USA) in blocking solution for 1 h at RT. Following washes, the protein bands were visualized using the Chemiluminescence Kit (Immun-Star™ WesternC™ Chemiluminescence Kit, Bio-Rad) on a Fujifilm Luminescent Image Analyzer LAS4000 system. The image analysis was performed with the Multi Gauge v3.0 program.

Mercier N., Pawelzik S.C., Pirault J., Carracedo M., Persson O., Wollensack B., Franco-Cereceda A, & Bäck M. (2020). Semicarbazide-Sensitive Amine Oxidase Increases in Calcific Aortic Valve Stenosis and Contributes to Valvular Interstitial Cell Calcification. Oxidative Medicine and Cellular Longevity, 2020, 5197376.

+ Open protocol

+ Expand

Protein Expression Profiling by Western Blot

Check if the same lab product or an alternative is used in the 5 most similar protocols

The tissue was homogenized in an SDS sample buffer containing a mixture of proteinase and phosphatase inhibitors (Sigma). The extracted protein (25 μg/μl) was separated on SDS–PAGE gels and transferred to nitrocellulose blots. The blots were blocked with 5% milk and incubated overnight at 4 °C with primary antibodies against cyclooxygenase-1 and 2 (COX-1, COX-2) (anti-COX-1 goat polyclonal antibody, 1:1000, cat# sc-1754, Santa Cruz Biotechnology Inc, Dallas, TX, USA and anti-COX-2 goat polyclonal antibody, 1:1000, cat# sc-1747, Santa Cruz Biotechnology Inc, Dallas, TX, USA). Endogenous β-actin was used as the loading control and was revealed using anti-human β-actin mouse monoclonal antibody (cat# MAB1501, EMD Millipore, Billerica, CA, USA). After incubation of the primary antibodies, the blots were washed and labeled with the respective secondary antibody, i.e. anti-mouse or anti-rabbit IgG (GE Healthcare Life Sciences) conjugated with horseradish peroxidase for 1 h at room temperature. Chemiluminescence detection was performed with an immobilon western chemiluminescent HRP substrate and measured directly using a BioSpectrum Imaging System (UVP). Specific bands were evaluated by apparent molecular size.

Wu P.C., Shieh D.B., Hsiao H.T., Wang J.C., Lin Y.C, & Liu Y.C. (2018). Magnetic field distribution modulation of intrathecal delivered ketorolac iron-oxide nanoparticle conjugates produce excellent analgesia for chronic inflammatory pain. Journal of Nanobiotechnology, 16, 49.

+ Open protocol

+ Expand

Quantitative Western Blot Analysis of Insulin Signaling

Check if the same lab product or an alternative is used in the 5 most similar protocols

Quantified, using the BCA protein assay kit (Thermo Fisher Scientific), equal amounts of protein were separated using 10% SDS-PAGE. After transfer to a nitrocellulose membrane (Schleicher & Schuell), milk-blocked blots were incubated with IRAP (#3808S; Cell Signaling Technology), GLUT4 (#2213; Cell Signaling Technology), GLUT3 (ab41525; Abcam), and actin antibody (#A2066; Sigma-Aldrich) overnight at a 1:1,000 dilution. Insulin signaling was investigated using the following primary antibodies: phosphorylated (Ser473)-AKT (#4051; Cell Signaling Technology), phosphorylated insulin receptor (Tyr1150/1150, #3024; Cell Signaling Technology), Pan-AKT (#2920; Cell Signaling Technology), and insulin receptor β (#3020; Cell Signaling Technology). Secondary incubation was done using anti–rabbit or anti–mouse IgG at a 1:2,000 dilution (GE Healthcare). Immunoreactivity was detected by the ECL detection system (GE Healthcare). The densitometric analyses of the immunoreactive bands were performed using ImageJ software (National Institutes of Health).

Ismail M.A., Mateos L., Maioli S., Merino-Serrais P., Ali Z., Lodeiro M., Westman E., Leitersdorf E., Gulyás B., Olof-Wahlund L., Winblad B., Savitcheva I., Björkhem I, & Cedazo-Mínguez A. (2017). 27-Hydroxycholesterol impairs neuronal glucose uptake through an IRAP/GLUT4 system dysregulation. The Journal of Experimental Medicine, 214(3), 699-717.

+ Open protocol

+ Expand

Western Blot Analysis of Irradiated Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols

After irradiation, lysates were obtained at various time points and sonicated (QSonica) for 2 minutes in 0.4 M NaCl/20 mM HEPES buffer containing 1% Igepal, 0.1 mM ethylene glycol tetraacetic acid and ethylenediaminetetraacetic acid, 0.1 M dithiothreitol, 0.1 M phenylmethanesulfonylfluoride, and protease and phosphatase inhibitors (Sigma). Protein concentrations were measured with a DC protein assay kit (Bio-Rad, Hercules, CA, USA). Equalized proteins were subjected to electrophoresis at 60 mA in polyacrylamide pre-cast gels (Bio-Rad) and electrotransferred onto polyvinylidene fluoride membranes (Bio-Rad) at 4ºC for 1 hour at 100 V. Membranes were blocked with 5% milk (Bio-Rad). Antibodies were incubated overnight in 5% milk at various concentrations (P16, BD Bioscience, 1:5000; TRIP12, Santa Cruz, 1:1000; RNF168, Sigma, 1:1000; pRb, CST, 1:500; Rb, CST, 1:1000). Membranes were washed in Tris-buffered saline (Bio-Rad) with 0.1% Tween20 (Sigma) and incubated for 45 minutes at ambient temperature in 1:2000 anti-rabbit or anti-mouse IgG (GE Healthcare). Immunoreactions were visualized with the ECL2 system (Thermo Scientific) and then immediately exposed to autoradiographic film (Denville) for various periods. Images were scanned with an HP Scanjet 5550c and quantified with ImageJ software (http://rsbweb.nih.gov/ij/).

Wang L., Zhang P., Molkentine D.P., Chen C., Molkentine J.M., Piao H., Raju U., Zhang J., Valdecanas D.R., Tailor R.C., Thames H.D., Buchholz T.A., Chen J., Ma L., Mason K.A., Ang K.K., Meyn R.E, & Skinner H.D. (2016). TRIP12 as a mediator of human papillomavirus/p16-related radiation enhancement effects. Oncogene, 36(6), 820-828.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!