Goat anti mouse or goat anti rabbit secondary antibodies

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Goat anti-mouse or goat anti-rabbit secondary antibodies are affinity-purified antibodies produced in goats and directed against mouse or rabbit primary antibodies. These secondary antibodies are commonly used in immunoassays and Western blotting applications to detect and quantify the presence of target proteins.

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Anti-mouse or anti-rabbit secondary antibodies (4 citations) Anti-mouse secondary antibodies (2 citations) IRDye 800CW goat anti-rabbit or goatanti-mouse secondary antibodies (2 citations) Goat anti-rabbit or goat anti-mouse IgG secondary antibodies (2 citations) IRDye 800CW Goat anti-mouse or anti-rabbit secondary antibodies (2 citations)

6 protocols using goat anti mouse or goat anti rabbit secondary antibodies

Western Blot Analysis of SWI/SNF Proteins

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Total protein was denatured for 10 min at 95 °C, separated on a 4–12% SDS-polyacrylamide gel, and transferred to a PVDF membrane (Immobilon FL, EMD Millipore, Billerica, MA). The membrane was blocked with 5% bovine serum albumin (VWR, Batavia, IL) in PBS containing 0.1% Tween-20 (PBST) for 30 mins at room temperature and then incubated in primary antibodies overnight at 4°C. The primary antibodies used were directed against ARID1A (Santa Cruz Biotechnology Inc., Dallas, TX; sc-32761), PBRM1 (Bethyl Laboratories, Montgomery, TX; A301–591A), BAF155 (Santa Cruz Biotechnology Inc., Dallas, TX; Sc-32763), BAF47 (Santa Cruz Biotechnology Inc., Dallas, TX; Sc-166165), LAMIN B1 (Santa Cruz Biotechnology Inc., Dallas, TX; Sc-377000). The primary antibodies were detected by incubating the membranes in goat-anti-rabbit or goat-anti-mouse secondary antibodies (LI-COR Biotechnology, Lincoln, NE) conjugated to IRDye 800CW or IRDye 680 respectively for 1 h at room temperature, and the signals were visualized using Odyssey Clx imager (LI-COR Biotechnology, Lincoln, NE).

Marian C.A., Stoszko M., Wang L., Leighty M.W., de Crignis E., Maschinot C.A., Gatchalian J., Carter B.C., Chowdhury B., Hargreaves D.C., Duvall J.R., Crabtree G.R., Mahmoudi T, & Dykhuizen E.C. (2018). Small Molecule Targeting of Specific BAF (mSWI/SNF) complexes for HIV Latency Reversal. Cell chemical biology, 25(12), 1443-1455.e14.

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Western Blot Analysis of Protein Samples

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Protein samples were mixed with 4x lithium dodecyl sulfate sample buffer containing 10% 2-merchaptoethanol. The protein lysates were denatured for 5 min at 95°C, separated on a 4–12% SDS-polyacrylamide gel, and transferred to a PVDF membrane (Immobilon FL, EMD Millipore, Billerica, MA). The membrane was blocked with 5% bovine serum albumin (VWR, Batavia, IL) in PBS containing 0.1% Tween-20 for one hour at room temperature and then incubated in primary antibodies overnight at 4°C. The primary antibodies were detected by incubating the membranes in goat anti-rabbit or goat anti-mouse secondary antibodies (LI-COR Biotechnology, Lincoln, NE) conjugated to IRDye 800CW or IRDye 680CW, respectively, for one hour at room temperature, and the signals were visualized using Odyssey Clx imager (LI-COR Biotechnology). Antibodies used for immunoblot: PBRM1 (Bethyl, A301-590A, 1:1000), ARID1A (Santa Cruz 1:1000) V5 (CST, D3H8Q, 1:1000), hnRNP A1 (Santa Cruz, 4B10 1:1000).

De Silva S.M., Dhiman A., Sood S., Mercedes K.F., Simmons W.J., Henen M.A., Vögeli B., Dykhuizen E.C, & Musselman C.A. (2023). PBRM1 bromodomains associate with RNA to facilitate chromatin association. Nucleic Acids Research, 51(8), 3631-3649.

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Cellular Response to Zinc Oxide Nanoparticles

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PERK, pPERK, IRE, CHOP, pJNK, BIP, and Caspase-3 antibodies were purchased from Cell Signaling Technology® (Danvars, MA). GCLC, pIRE, ATF6 (90 kd) and diluted to a concentration of 1:1000, and XBP1 antibodies were purchased from Abcam Biotechnology and was used at 2 μg/ml (Cambridge, MA). Actin antibody was purchased from Sigma Aldrich (St. Louis, MO). The RAECs were exposed to pristine, annealed, oxidized or reduced ZnO NPs (20 μg/mL) for 6, 12, and 24 h in 100 mm dishes. The cells were washed with cold PBS, scraped, and pelleted. The pellets were lysed with 1% SDS and 80 mM Tris HCl containing protease and phosphatase inhibitor cocktails purchased from Sigma Aldrich (Sigma Aldrich, St. Louis, MO, USA). Samples were loaded into 12% tris-glycine gels (Thermo Fisher Scientific, MO, USA) to separate the proteins based on their size. The membranes were probed using antibodies listed above and exposed to goat anti-mouse or goat anti-rabbit secondary antibodies purchased from LiCor Biosciences and imaged using an Odyssey Infrared Imaging System (NE, USA). ImageJ software (NIH) was used for densiometric analysis and normalized with the corresponding actin band.

Persaud I., Raghavendra A.J., Paruthi A., Alsaleh N.B., Minarchick V.C., Roede J.R., Podila R, & Brown J.M. (2019). Defect-Induced Electronic States Amplify the Cellular Toxicity of ZnO Nanoparticles. Nanotoxicology, 14(2), 145-161.

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Quantitative Western Blot Analysis

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Sem7a western blots were performed by loading equal amounts of protein into each lane. Protein concentration in lysates was determined by Bradford assay. Blots were probed with anti-Sema7a (Atlas) or anti-COX2 (Cayman) primary antibodies, and goat anti-mouse or goat anti-rabbit secondary antibodies (LICOR). Blots were imaged and quantitated on an Odyssey CLx Imager (LICOR).

Black S., Nelson A.C., Gurule N., Futscher B.W, & Lyons T.R. (2016). Semaphorin 7a exerts pleiotropic effects to promote breast tumor progression. Oncogene, 35(39), 5170-5178.

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Quantitative Western Blot Analysis

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Black S., Nelson A.C., Gurule N., Futscher B.W, & Lyons T.R. (2016). Semaphorin 7a exerts pleiotropic effects to promote breast tumor progression. Oncogene, 35(39), 5170-5178.

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Tau Protein Effects on Squid Axoplasm

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Lysates were prepared from “sister” axoplasms as described (Kang et al., 2016 (link)). Briefly, two axons from an individual squid were dissected and extruded onto glass slides. One axoplasm was perfused with a Control perfusion mix (Buffer X/2) and the other with an Experimental perfusion mix (5 μM Tau recombinant protein). After 50 min incubation, axoplasms were collected in 1% SDS and 6× sample buffer in preparation for immunoblotting.
Squid axoplasm lysates were run on 4–12% Bis/Tris gels (Invitrogen) in MOPS buffer and proteins were transferred to PVDF membrane (Bio-Rad) using Towbin buffer with 10% methanol. Membranes were dried for at least 1 h before being reactivated in methanol and blocked in 1% milk in TBS supplemented with 2 mM Sodium Orthovanadate and 10 mM Sodium Fluoride to block phosphatase activity present in milk. Primary antibodies were incubated overnight diluted in 1% BSA in TBS supplemented as before. Goat anti-mouse or goat anti-rabbit secondary antibodies (LiCor) were incubated for 1 h at RT and immunoblots visualized using a LiCor Odyssey Fc imaging system. LiCor ImageStudio Lite was used for quantitation of signal intensity.

Morris S.L., Tsai M.Y., Aloe S., Bechberger K., König S., Morfini G, & Brady S.T. (2021). Defined Tau Phosphospecies Differentially Inhibit Fast Axonal Transport Through Activation of Two Independent Signaling Pathways. Frontiers in Molecular Neuroscience, 13, 610037.

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