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PMycB is a laboratory equipment designed for the detection and quantification of mycotoxins in various samples. It utilizes a proprietary method to accurately measure the presence and concentration of these fungal toxins.

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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) Anti c myc antibodies, by Enzo Life Sciences (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 pmycb

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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