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Anti c myc antibodies

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Anti-c-Myc antibodies are a type of laboratory reagent used for the detection and study of the c-Myc protein. The c-Myc protein is a transcription factor that plays a critical role in cellular processes such as cell growth, proliferation, and differentiation. These antibodies can be used in various techniques, including Western blotting, immunoprecipitation, and immunocytochemistry, to identify and quantify the c-Myc protein in biological samples.

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Lab products found in correlation

Anti rabbit igg hrp, by Bio-Rad (2 mentions) Anti mouse igg hrp, by Bio-Rad (2 mentions) Pmycb, by Santa Cruz Biotechnology (2 mentions) Anti rabbit pan actin polyclonal antibody, by Cell Signaling Technology (2 mentions) Anti caspase 1 p10 sc 514, by Santa Cruz Biotechnology (2 mentions) Anti flag m2 f1804, by Merck Group (2 mentions) Lipofectamine 2000, by Thermo Fisher Scientific (2 mentions)

2 protocols using anti c myc antibodies

1

Analyzing NLRC4 Inflammasome Activation in HEK293 Cells

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NLRC4 activity was analyzed in HEK293-cells. Wild-type human NLRC4 was cloned into pMycB (Santa Cruz Biotech) and verified by Sanger sequencing. The c.1022 T->C mutation was introduced by site-directed mutagenesis (Stragene QuikChange) and verified by Sanger sequencing. Mutated and wildtype myc-NLRC4 were transiently transfected into HEK293 cells along with N-terminal FLAG-human pro-caspase-1 and GFP-tagged human ASC using Lipofectamine2000 (Invitrogen). NLRC4 activity was visually measured 30h after transfection by spontaneous formation of GFP-ASC foci (as visualized in live cells by epifluorescent microscopy). Manual enumeration of ASC foci+ was performed over 20 representative fields at 20x magnification. Pro-caspase-1 p45 autoproteolysis was measured directly by western blotting for p35 (anti-FLAG M2 (F1804), 1:1000; Sigma) and p10 fragments (anti-caspase-1 p10 (sc-514), 1:200; Santa Cruz Biotech), using anti-mouse IgG-HRP or anti-rabbit IgG-HRP (Biorad) and enhanced chemiluminescence. The presence of NLRC4 and actin in lysates was confirmed by blotting with anti- c-Myc antibodies (9E10, 1:1000; Enzo Life Sciences) or anti-rabbit pan-actin polyclonal antibody (#4970, 1:5000; Cell Signaling Technology), respectively.
Romberg N., Al Moussawi K., Nelson-Williams C., Stiegler A.L., Loring E., Choi M., Overton J., Meffre E., Khokha M.K., Huttner A.J., West B., Podoltsev N.A., Boggon T.J., Kazmierczak B.I, & Lifton R.P. (2014). Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation. Nature genetics, 46(10), 1135-1139.
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2

Analyzing NLRC4 Inflammasome Activation in HEK293 Cells

Check if the same lab product or an alternative is used in the 5 most similar protocols
NLRC4 activity was analyzed in HEK293-cells. Wild-type human NLRC4 was cloned into pMycB (Santa Cruz Biotech) and verified by Sanger sequencing. The c.1022 T->C mutation was introduced by site-directed mutagenesis (Stragene QuikChange) and verified by Sanger sequencing. Mutated and wildtype myc-NLRC4 were transiently transfected into HEK293 cells along with N-terminal FLAG-human pro-caspase-1 and GFP-tagged human ASC using Lipofectamine2000 (Invitrogen). NLRC4 activity was visually measured 30h after transfection by spontaneous formation of GFP-ASC foci (as visualized in live cells by epifluorescent microscopy). Manual enumeration of ASC foci+ was performed over 20 representative fields at 20x magnification. Pro-caspase-1 p45 autoproteolysis was measured directly by western blotting for p35 (anti-FLAG M2 (F1804), 1:1000; Sigma) and p10 fragments (anti-caspase-1 p10 (sc-514), 1:200; Santa Cruz Biotech), using anti-mouse IgG-HRP or anti-rabbit IgG-HRP (Biorad) and enhanced chemiluminescence. The presence of NLRC4 and actin in lysates was confirmed by blotting with anti- c-Myc antibodies (9E10, 1:1000; Enzo Life Sciences) or anti-rabbit pan-actin polyclonal antibody (#4970, 1:5000; Cell Signaling Technology), respectively.
Romberg N., Al Moussawi K., Nelson-Williams C., Stiegler A.L., Loring E., Choi M., Overton J., Meffre E., Khokha M.K., Huttner A.J., West B., Podoltsev N.A., Boggon T.J., Kazmierczak B.I, & Lifton R.P. (2014). Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation. Nature genetics, 46(10), 1135-1139.
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