Control rabbit igg

Manufactured by Jackson ImmunoResearch

Sourced in United States

Control rabbit IgG is a purified immunoglobulin G (IgG) fraction isolated from non-immunized rabbit serum. It serves as a control for experiments involving rabbit antibodies.

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Lab products found in correlation

Protein a beads, by Repligen (1 mentions) Bioruptor sonicator, by Cosmo Bio (1 mentions) Protein g sepharose beads, by Merck Group (1 mentions)

4 protocols using control rabbit igg

Immunoprecipitation of V5-tagged Proteins

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Male and female mice were deeply anesthetized with isofluorane vapor before rapid decapitation. Whole brains were quickly transferred to a solution of 1% Triton X-100 buffer with protease inhibitors and homogenized via a mortar and pestle. The homogenate was then spun at 90,000 g for 30 min at 4 C to remove debris. The resulting supernatant was then collected and pre-cleared with 0.1% Triton X-100 washed protein-A beads (RepliGen Cat # 10-1003-01) for 1 h at 4 C. A small portion of pre-cleared supernatant was saved for input, and the remaining supernatant was then incubated with 2 µg of Rabbit anti-V5-tag antibody (Cell Signaling Technology Cat# 13202) or 2 µg of control rabbit IgG (Jackson ImmunoResearch Cat# 309-005-008) and 30 µL of protein-A beads for 4 h rotating head over tail at 4 C. The antibody bound beads were then washed three times with 0.1% Triton X-100 and pelleted to isolate the protein bound beads. The supernatant was then removed and the bead bound proteins were eluted with 100 µL of 1x sample buffer and boiled for 5 min at 100 C.

Lloyd B.A., Han Y., Roth R., Zhang B, & Aoto J. (2023). Neurexin-3 subsynaptic densities are spatially distinct from Neurexin-1 and essential for excitatory synapse nanoscale organization in the hippocampus. Nature Communications, 14, 4706.

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ChIP Assay for GLI1 Binding

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ChIP assays were performed essentially as described previously.38 B16F10 cells were cross‐linked with formaldehyde, lysed, and sonicated using a Bioruptor sonicator (CosmoBio, Tokyo, Japan). The lysates were immunoprecipitated with the rabbit anti‐GLI1 H300 Ab (sc‐20687; Santa Cruz Biotechnology) or control rabbit IgG (011‐000‐003; Jackson ImmunoResearch Laboratory, West Grove, PA, USA), and the precipitated DNA was subjected to quantitative PCR (qPCR). Primers used for the qPCR are listed in Table S3.

Gunarta I.K., Li R., Nakazato R., Suzuki R., Boldbaatar J., Suzuki T, & Yoshioka K. (2017). Critical role of glioma‐associated oncogene homolog 1 in maintaining invasive and mesenchymal‐like properties of melanoma cells. Cancer Science, 108(8), 1602-1611.

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Quantifying Surface Glycans and Antibody Binding

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Overnight cultures were centrifuged and resuspended in HEPES++buffer (20 mM HEPES, 140 mM NaCl, 5 mM CaCl₂, 2.5 mM MgCl₂, pH 7.4) + 0.1% bovine serumalbumin (BSA) (HEPES++0.1%BSA) to OD₆₀₀=0.4. The bacterial suspension (100 μl) was pelleted and stained with FITC-labeled succinylated wheat germ agglutinin (sWGA) to assess GlcNAc expression. M1 protein expression was quantified on bacterial cultures at an OD₆₀₀ = 0.6 using anti-M1 or sham mouse serum and PE-conjugated anti-mouse IgG. To test IgG binding, bacterial cultures were grown to OD₆₀₀ of 0.4, washed, resuspended in buffer and pre-incubated with 10% heat-inactivated normal horse serum to block Fc binding proteins. After washing, samples were incubated with 0.1 mg/ml control rabbit IgG (Jackson Immunoresearch) or purified anti-ΔGAC rabbit IgG followed by allophycocyanin-conjugated goat anti-rabbit IgG. Staining was analyzed by flow cytometry.

van Sorge N.M., Cole J.N., Kuipers K., Henningham A., Aziz R.K., Kasirer-Friede A., Lin L., Berends E.T., Davies M.R., Dougan G., Zhang F., Dahesh S., Shaw L., Gin J., Cunningham M., Merriman J.A., Hütter J., Lepenies B., Rooijakkers S.H., Malley R., Walker M.J., Shattil S.J., Schlievert P.M., Choudhury B, & Nizet V. (2014). The Classical Lancefield Antigen of Group A Streptococcus is a Virulence Determinant with Implications for Vaccine Design. Cell host & microbe, 15(6), 729-740.

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Nucleolin Interaction Profiling in Pancreatic Cancer

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A total of 8 × 10⁶ MIA PaCa-2 and Panc-1 cells were plated in 75 cm² flasks. The day after, cells were stimulated or not with Wnt3a-CM for 3 h, and lysed using the same lysis buffer as for the pull-down. One mg of proteins of the extra-nuclear fraction was incubated with 5 µg rabbit anti-nucleolin antibody (Abcam ab22758) or 5 µg control rabbit IgG (Jackson, 011-000-002) for 1 h at 4 °C by mixing samples. Protein G sepharose beads (Millipore, Burlington, MA, USA) were prepared and added to the protein/antibody solution, according to the manufacturer’s instructions. After washing, the proteins were eluted and analyzed by Western blotting.

Raineri F., Bourgoin-Voillard S., Cossutta M., Habert D., Ponzo M., Houppe C., Vallée B., Boniotto M., Chalabi-Dchar M., Bouvet P., Couvelard A., Cros J., Debesset A., Cohen J.L., Courty J, & Cascone I. (2021). Nucleolin Targeting by N6L Inhibits Wnt/β-Catenin Pathway Activation in Pancreatic Ductal Adenocarcinoma. Cancers, 13(12), 2986.

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