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Secondary anti mouse and anti rabbit antibodies

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Secondary anti-mouse and anti-rabbit antibodies are laboratory reagents used in immunodetection assays, such as Western blotting and immunohistochemistry, to detect and quantify target proteins. These antibodies bind to the primary antibodies that recognize the target proteins, allowing for signal amplification and visualization of the target analytes.

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Lab products found in correlation

Odyssey clx infrared imaging system, by LI COR (3 mentions) P egfr, by Cell Signaling Technology (2 mentions) β actin, by Merck Group (2 mentions) P erk1 2, by Cell Signaling Technology (2 mentions) Penicillin streptomycin, by Thermo Fisher Scientific (2 mentions) Gapdh, by Cell Signaling Technology (2 mentions) Rpmi 1640 medium, by Thermo Fisher Scientific (2 mentions) Rabbit anti akt, by Cell Signaling Technology (1 mentions) Anti caspase 3, by Cell Signaling Technology (1 mentions) Odyssey blocking buffer tbs, by LI COR (1 mentions) Radioimmunoprecipitation assay buffer, by Merck Group (1 mentions) Cleaved parp, by Cell Signaling Technology (1 mentions) Cleaved caspase 3, by Cell Signaling Technology (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Anti caspase 8, by Cell Signaling Technology (1 mentions) β actin, by Cell Signaling Technology (1 mentions) Erk1 2, by Santa Cruz Biotechnology (1 mentions) Proliferating cell nuclear antigen (pcna), by Santa Cruz Biotechnology (1 mentions) P atr, by Cell Signaling Technology (1 mentions) P chk2, by Cell Signaling Technology (1 mentions)

Close spelling variants of this product

Donkey anti-mouse IRDye 800CW and goat anti-rabbit IRDye 680RD secondary antibodies Goat anti-mouse immunoglobulin G (IgG) and goat anti-rabbit IgG secondary antibodies Secondary IRDye-labeled goat anti-mouse and anti-rabbit IgG antibodies Anti-mouse immunoglobulin G and anti-rabbit immunoglobulin G fluorescent-conjugated secondary antibodies IRDye680LT- and IRDye800-conjugated anti-rabbit and anti-mouse IgG secondary antibodies IRDye donkey anti-rabbit 800 and goat anti-mouse 680 secondary antibodies IRDye 800CW goat anti-mouse and anti-rabbit secondary antibodies Anti-mouse or anti-rabbit HRP-conjugated or IR-680 and IR-800 dye-conjugated secondary antibodies IRDye 800CW anti-rabbit and anti-mouse secondary antibodies Fluorescently labeled anti-mouse and anti-rabbit secondary antibodies

14 protocols using secondary anti mouse and anti rabbit antibodies

1

Western Blot Analysis of Kidney Signaling

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Snap frozen kidney tissue was homogenized and tissue lysates or cell culture lysates were resolved by SDS–polyacrylamide gel electrophoresis, transferred to nitrocellulose membranes, and probed with primary antibodies. Mouse anti-Phospho-p70-S6K (Thr389), rabbit anti-p70-S6K mouse anti-Phospho-Erk1/2 (Thr202/Tyr24), rabbit anti-Erk1/2, rabbit anti-Phospho-AMPKα (Thr172), mouse-anti-Phospho-Akt (Ser473), rabbit anti-Akt and anti-caspase-3 antibodies were obtained from Cell signaling Technology, Beverly, MA, USA. Mouse anti-AMPKα was obtained from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Anti-mouse and anti-rabbit secondary antibodies were purchased from Licor Biosciences (Lincoln, Nebraska, USA).
Riwanto M., Kapoor S., Rodriguez D., Edenhofer I., Segerer S, & Wüthrich R.P. (2016). Inhibition of Aerobic Glycolysis Attenuates Disease Progression in Polycystic Kidney Disease. PLoS ONE, 11(1), e0146654.
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2

Western Blot Protein Detection

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Tissue was pulverized in LN2 and homogenized by sonication on ice in radioimmunoprecipitation assay buffer (Sigma-Aldrich, St. Louis, MO). After denaturation in loading buffer, samples were separated by and blotted to nitrocellulose membranes. Membranes were blocked in TBS Odyssey Blocking Buffer (LI-COR, Lincoln, NE) before being incubated overnight with primary rabbit, anti-mouse antibodies for the proteins of interest. Proteins were detected by infrared fluorescent detection (LI-COR Odyssey) using appropriate anti-mouse and anti-rabbit secondary antibodies (LI-COR).
Zabielski P., Lanza I.R., Gopala S., Holtz Heppelmann C.J., Bergen HR I.I.I., Dasari S, & Nair K.S. (2015). Altered Skeletal Muscle Mitochondrial Proteome As the Basis of Disruption of Mitochondrial Function in Diabetic Mice. Diabetes, 65(3), 561-573.
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3

Apoptosis and DNA Damage Analysis

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Attached cells treated with inhibitor and/or radiation were washed with 1X ice cold PBS 24 hours post-treatment. Protein lysate buffer containing a cocktail of protease inhibitors and cells were scraped off into a tube on ice. The cells were incubated on ice for 10 minutes. Cell lysates were separated by SDS-PAGE and electrophoretically transferred to PVDF membranes. The membranes were blocked before anti-caspase 8 (Cell signaling), p53 (Cell Signaling), cleaved PARP (Cell Signaling), cleaved caspase 3 (Cell signaling), p21 (Cell Signaling), 53BP1 (Cell Signaling). and β-actin (Cell signaling) were applied at 1:5000 dilution. Anti-mouse and anti-rabbit secondary antibodies were then employed (LI-COR Biosciences, Lincoln, NE, USA). Signals were measured using the Odyssey Infrared Imaging system (LI-COR Biosciences) and quantified using LICOR software.
Chitsike L., Bertucci A., Vazquez M., Lee S., Unternaehrer J.J, & Duerksen-Hughes P.J. (2023). GA-OH enhances the cytotoxicity of photon and proton radiation in HPV+ HNSCC cells. Frontiers in Oncology, 13, 1070485.
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4

Western Blot Analysis of Cellular Proteins

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Proteins from whole-cell extracts were detected by Western blot according to standard protocols. The Odyssey® CLx Infrared Imaging System (LI-COR Biosciences) was used for signal detection and quantification. Primary antibodies: EGFR (1:1000, rabbit, Cell Signaling, #2232); pEGFR (1:1000, rabbit, Cell Signaling, #4407); β-Actin (1:20,000, mouse, Sigma-Aldrich, #A-2228); MLH1 (1:1000, Cell Signaling, #3515); MSH2 (1:1000, Cell Signaling, #2850); MSH6 (1:1000, Cell Signaling, #4407); MSH3 (1:1000, BD Transduction Laboratories, #611390); PMS2 (1:1000, Rockland, #29379); PCNA (1:1000, Santa Cruz Biotechnology, sc-56); ERK1/2 (1:1000. Cell Signaling, #9107); pERK1/2 (1:1000. Cell Signaling, #4370); p38 (1:1000, Cell Signaling, #8690); pp38 (1:1000, Cell Signaling, #4511); JNK (1:1000. Cell Signaling, #9252), pJNK (1:1000. BD Transduction Laboratories, #612540). All primary antibodies were diluted in 5% bovine serum albumine (BSA) in PBS supplemented with 0.2% Tween. Secondary anti-mouse and anti-rabbit antibodies were purchased from LI-COR Biosciences.
Struve N., Binder Z.A., Stead L.F., Brend T., Bagley S.J., Faulkner C., Ott L., Müller-Goebel J., Weik A.S., Hoffer K., Krug L., Rieckmann T., Bußmann L., Henze M., Morrissette J.J., Kurian K.M., Schüller U., Petersen C., Rothkamm K., O´ Rourke D.M., Short S.C, & Kriegs M. (2020). EGFRvIII upregulates DNA mismatch repair resulting in increased temozolomide sensitivity of MGMT promoter methylated glioblastoma. Oncogene, 39(15), 3041-3055.
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5

Western Blot Analysis of DNA Damage Response Proteins

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Proteins from whole-cell extracts were detected by WB according to standard protocols. The Odyssey CLx Infrared Imaging System (LI-COR Biosciences) was used for signal detection and quantification. Primary antibodies: EGFR (1:1000, rabbit, Cell Signaling Technology, #2232); pEGFR (1:1000, rabbit, Cell Signaling Technology, #4407); β-Actin (1:40000, mouse, Sigma-Aldrich, #A-2228); ATM (1:1000, rabbit, Cell Signaling Technology, #2873); pATM (1:1000, rabbit, GeneTex, GTX61739); ATR (1:1000, mouse, Santa Cruz, #SC-515173); pATR (1:1000, rabbit, Cell Signaling Technology, #58014); Chk1 (1:1000, mouse, Cell Signaling Technology, #2360); pChk1 (1:1000, rabbit, US Biological, #C4200-05); Chk2 (1:1000, mouse, BD Transduction Laboratories, #2360); pChk2 (1:1000, rabbit, Cell Signaling Technology, #2661); RPA (1:1000, mouse, Santa Cruz, SC-56770); pRPA (1:1000, rabbit, Boster, #02067); RNaseH (1:1000, rabbit, Abcam, #ab229078). All primary antibodies were diluted in 5% bovine serum albumin (BSA) in PBS supplemented with 0.2 % Tween. Secondary anti-mouse and anti-rabbit antibodies were purchased from LI-COR Biosciences.
Struve N., Hoffer K., Weik A.S., Riepen B., Krug L., Cetin M.H., Burmester J., Ott L., Liebing J., Gatzemeier F., Müller-Goebel J., Gerbach M., Bußmann L., Parplys A.C., Unger K., Mansour W.Y., Schüller U., Rieckmann T., Petersen C., Rothkamm K., Short S.C, & Kriegs M. (2021). Increased replication stress and R-loop accumulation in EGFRvIII-expressing glioblastoma present new therapeutic opportunities. Neuro-oncology Advances, 4(1), vdab180.
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6

Macrophage ABCA1 Regulation by Cholesterol and LXR

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Macrophages were incubated for 3 h with 100 μg CCs/ 1×106 cells and treated for 24 h with 10 mM CD. LXR agonist T0901317 (Sigma) was used as a positive control for LXR activation. Cells were lysed on ice for 30 min with 1x RIPA buffer (20 mM Tris-HCl pH 7.4, 150 mM NaCl, 1 mM EDTA, 1% Triton X-100, 10% glycerol, 0.1% SDS, 0.5% deoxycholate, 0.1 μM PMSF) supplemented with complete protease inhibitors (Roche Biochemicals). Protein concentrations were determined by BCA assay (Pierce) and equal amounts of protein were loaded on 4–12% pre-cast SDS-PAGE gels (Novex, Invitrogen) with MOPS running buffer (Novex, Invitrogen). Proteins were transferred to a PVDF membrane (Millipore) and membranes were blocked in 3% BSA in TBS with Tween-20, incubated with mouse monoclonal ABCA1 antibody (MAB10005, Millipore) and rabbit monoclonal β-actin antibody (Li-Cor Biosciences) overnight at 4°C. The membranes were washed and incubated with secondary anti-mouse and anti-rabbit antibodies (Li-Cor Biosciences) for 45 min in the dark. Immunoreactivity was visualized by near-infrared detection (Odyssey, LICOR).
Zimmer S., Grebe A., Bakke S.S., Bode N., Halvorsen B., Ulas T., Skjelland M., De Nardo D., Labzin L.I., Kerksiek A., Hempel C., Heneka M.T., Hawxhurst V., Fitzgerald M.L., Trebicka J., Gustafsson J.Å., Westerterp M., Tall A.R., Wright S.D., Espevik T., Schultze J.L., Nickenig G., Lütjohann D, & Latz E. (2016). Cyclodextrin promotes atherosclerosis regression via macrophage reprogramming. Science translational medicine, 8(333), 333ra50.
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7

Western Blot Analysis of EGFR Signaling

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Proteins from whole cell extracts were detected by Western blot according to standard protocols. The antibodies recognizing EGFR, pEGFR (Y1173), ERK, pERK (T202, Y204), AKT and pAKT (T308) were obtained from Cell Signaling Technology, while the anti β-Actin antibody was purchased from Sigma-Aldrich. The EGFRvIII antibody (clone L8A4) was kindly provided by D. Binger. Secondary anti-mouse and anti-rabbit antibodies were purchased from LI-COR Biosciences. The Odyssey® CLx Infrared Imaging System (LI-COR Biosciences) was used for signal detection and quantification.
Struve N., Riedel M., Schulte A., Rieckmann T., Grob T.J., Gal A., Rothkamm K., Lamszus K., Petersen C., Dikomey E, & Kriegs M. (2015). EGFRvIII does not affect radiosensitivity with or without gefitinib treatment in glioblastoma cells. Oncotarget, 6(32), 33867-33877.
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8

Ritonavir and GLUT Protein Analyses

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Ritonavir (Norvir) was obtained from Abbott pharmaceuticals (Abbott Park, IL). Ritonavir, in pure drug form and used for in vitro studies was provided by the NIH AIDS Reagent Program. GLUT1 and GLUT12 polyclonal antibodies were kind gifts from Mike Mueckler and Kelle Moley, respectively (Washington University, St. Louis, MO). GLUT4 antibody was custom produced by Invitrogen using a peptide corresponding to the 16 carboxyl-terminal residues of GLUT4. Human GLUT12 plasmid was obtained from the DNASU Plasmid Repository (Tempe, AZ). GAPDH monoclonal antibody was purchased from Sigma (St. Louis, MO). Secondary anti-mouse and anti-rabbit antibodies were from LI-COR (Lincoln, NE). Unless noted, all other reagents were purchased from Sigma (St. Louis, MO).
Heitmeier M.R., Payne M.A., Weinheimer C., Kovacs A., Hresko R.C., Jay P.Y, & Hruz P.W. (2018). Metabolic and Cardiac Adaptation to Chronic Pharmacologic Blockade of Facilitative Glucose Transport in Murine Dilated Cardiomyopathy and Myocardial Ischemia. Scientific Reports, 8, 6475.
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9

Protein Purification and Detection

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Samples from important steps during purification were collected and analysed by SDS-PAGE and western blot. TGX™ Precast Gel (BioRad) was used to separate proteins within samples at 200 V for 30 min. Then gels were either stained by Instant Blue (Sigma Aldrich) or immediately transferred to PVDF membrane (BioRad) at 100 V for 1 h. The proteins on the PVDF membrane were probed with two primary antibodies simultaneously, rabbit anti-Gs C-18 antibody (cat. no. sc-383, Santa Cruz) against Gαs subunit and mouse poly-His antibody (cat. no. 34660, QIAGEN) against His tags. The membrane was washed and incubated with secondary anti-mouse and anti-rabbit antibodies (LI-COR). The membranes were imaged on a Typhoon 5 imaging system (Amersham).
Zhang X., Belousoff M.J., Zhao P., Kooistra A.J., Truong T.T., Ang S.Y., Underwood C.R., Egebjerg T., Šenel P., Stewart G.D., Liang Y., Glukhova A., Venugopal H., Christopoulos A., Furness S.G.B., Miller L.J., Reedtz‐Runge S., Langmead C.J., Gloriam D.E., Danev R., Sexton P.M., & Wootten D. (2020). Differential GLP-1R binding and activation by peptide and non-peptide agonists.
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10

Quantitative Assessment of EP Receptor Expression

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OPCs from cultures were rinsed in PBS and subsequently lysed in SDS sample buffer containing protease inhibitors (cOmplete ULTRA®-protease inhibitor, Roche, Mannheim, Germany). The samples were fractionated on a 10 % acrylamide gel by electrophoresis, then electro blot transferred to nitrocellulose and probed with the same rabbit antibodies to EP1–EP4 (used at a dilution of 1:200) along with mouse anti-oligodendrocyte-specific protein (OSP) (used at a dilution of 1:400) to normalize for loading. The blot was washed and then probed with anti-rabbit and anti-mouse secondary antibodies (Licor Biotechnology, Lincoln, NE) (used at a dilution of 1:5000) and visualized using the Li-COR imaging system. Densitometry scanning of the Western blot image files was performed using image J to quantify the relative intensity of each EP receptor, and this was normalized to OSP for each lane. The relative amounts were quantified from triplicate gels and assessed for statistical differences using ANOVA, Tukey-Kramer multiple comparison test.
Carlson N.G., Bellamkonda S., Schmidt L., Redd J., Huecksteadt T., Weber L.M., Davis E., Wood B., Maruyama T, & Rose J.W. (2015). The role of the prostaglandin E2 receptors in vulnerability of oligodendrocyte precursor cells to death. Journal of Neuroinflammation, 12, 101.
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