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Anti pyrin

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Anti-pyrin is a laboratory equipment product. It is designed for the detection and measurement of pyrin, a protein involved in inflammatory processes. The core function of Anti-pyrin is to facilitate the analysis of pyrin levels in biological samples.

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Lab products found in correlation

Mini protease inhibitor mixture, by Roche (3 mentions) Transblot turbo midi size pvdf membranes, by Bio-Rad (3 mentions) Anti flag, by Merck Group (3 mentions) Anti flag m2 affinity gel, by Merck Group (3 mentions) Sodium fluoride, by Merck Group (3 mentions) Actin, by Cell Signaling Technology (2 mentions) Cleaved il 1β, by Cell Signaling Technology (2 mentions) Il 1β, by Cell Signaling Technology (2 mentions) Ha tag, by Cell Signaling Technology (2 mentions) Flag tag (flag), by Merck Group (2 mentions) Anti asc, by Santa Cruz Biotechnology (2 mentions) Anti human caspase 1, by Santa Cruz Biotechnology (2 mentions) Anti phospho s242 pyrin, by Abcam (2 mentions) Anti human gsgmd, by Merck Group (2 mentions) Anti β actin clone, by Merck Group (2 mentions) Acrylamide gel, by Bio-Rad (2 mentions) Anti human il 1β, by Cell Signaling Technology (2 mentions) Ab200420, by Abcam (1 mentions) Anti β actin clone c4, by Merck Group (1 mentions)

5 protocols using anti pyrin

1

Immunoprecipitation and Western Blot Analysis of Pyrin

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Cells were lysed in 25 mM Tris–HCl, 150 mM NaCl, 1 mM EDTA, and 0.1% NP‐40 buffer containing Mini Protease Inhibitor Mixture (Roche) and sodium fluoride (Sigma) by a quick freezing and thawing step. Flag‐Pyrin was immuno‐precipitated using anti‐Flag M2 affinity gel (Sigma). Proteins were separated by SDS–PAGE on precast 4–15% acrylamide gels (Bio‐Rad) and transferred to TransBlot® Turbo™ Midi‐size PVDF membranes (Bio‐Rad). Antibodies used were mouse monoclonal anti‐FLAG® (Sigma‐Aldrich, clone M2; 1:1,000 dilution), anti‐Pyrin (Adipogen, AL196, 1: 1,000 dilution), anti‐phospho S242 Pyrin (Abcam, ab200420; 1:1,000 dilution; Gao et al, 2016), and anti‐PKN1 (Becton Dickinson, BD 610687; 1:1,000 dilution). Cell lysates were reprobed with a mouse monoclonal antibody anti‐β‐actin (clone C4, Millipore; 1:5,000 dilution). Full Western blot images are presented in Source Data.
Magnotti F., Lefeuvre L., Benezech S., Malsot T., Waeckel L., Martin A., Kerever S., Chirita D., Desjonqueres M., Duquesne A., Gerfaud‐Valentin M., Laurent A., Sève P., Popoff M., Walzer T., Belot A., Jamilloux Y, & Henry T. (2019). Pyrin dephosphorylation is sufficient to trigger inflammasome activation in familial Mediterranean fever patients. EMBO Molecular Medicine, 11(11), e10547.
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2

Investigating Genetic Variants in Inflammasome Pathways

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PCR amplification from cDNAs of the THP-1 cell line and healthy control PBMCs was used to construct human WT ASC, caspase1, MEFV, and IL-1β plasmids. Site-directed mutagenesis was used to generate the mutation plasmids. Western blotting and IF were performed using various antibodies, including anti-pyrin (Adipogen, rabbit, AL196), -ASC (Cell Signaling Technology, rabbit, 13833), –IL-1β (Cell Signaling Technology, rabbit, 12703), –Cleaved IL-1β (Cell Signaling Technology, rabbit, 83186), –14-3-3 (Santa Cruz Biotechnology Inc., mouse, sc-25276), -Actin (Cell Signaling Technology, mouse, 3700), –Flag-tag (MilliporeSigma, mouse, F1804), and –HA-tag (Cell Signaling Technology, rabbit, C29F4).
Wang Q., Jin T., Jian S., Han X., Song H., Zhou Q, & Yu X. (2023). A dominant pathogenic MEFV mutation causes atypical pyrin-associated periodic syndromes. JCI Insight, 8(19), e172975.
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3

Investigating Genetic Variants in Inflammasome Pathways

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PCR amplification from cDNAs of the THP-1 cell line and healthy control PBMCs was used to construct human WT ASC, caspase1, MEFV, and IL-1β plasmids. Site-directed mutagenesis was used to generate the mutation plasmids. Western blotting and IF were performed using various antibodies, including anti-pyrin (Adipogen, rabbit, AL196), -ASC (Cell Signaling Technology, rabbit, 13833), –IL-1β (Cell Signaling Technology, rabbit, 12703), –Cleaved IL-1β (Cell Signaling Technology, rabbit, 83186), –14-3-3 (Santa Cruz Biotechnology Inc., mouse, sc-25276), -Actin (Cell Signaling Technology, mouse, 3700), –Flag-tag (MilliporeSigma, mouse, F1804), and –HA-tag (Cell Signaling Technology, rabbit, C29F4).
Wang Q., Jin T., Jian S., Han X., Song H., Zhou Q, & Yu X. (2023). A dominant pathogenic MEFV mutation causes atypical pyrin-associated periodic syndromes. JCI Insight, 8(19), e172975.
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4

Pyrin-ASC Inflammasome Activation

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Cells were lysed in 25mM Tris HCl, 150mM NaCl, 1mM EDTA and 0.1% NP-40 buffer containing Mini Protease Inhibitor Mixture (Roche) and sodium fluoride (Sigma) by a quick freezing and thawing step. Flag-Pyrin was immuno-precipitated using anti Flag M2 affinity gel (Sigma). ASC was cross-linked in the insoluble pellet using DSS (Disuccinimidyl suberate, ThermoFisher #21655) 2 mM (1 h at 37°C). Proteins were separated by SDS/PAGE on precast 4–15% acrylamide gels (Bio-rad) and transferred to TransBlot® Turbo™ Midi-size PVDF membranes (Bio-rad). Antibodies used were mouse monoclonal anti-FLAG® (Sigma-Aldrich, clone M2; 1:1,000 dilution), anti-Pyrin (Adipogen, AL196, 1: 1,000 dilution), anti-phospho S242 Pyrin (Abcam, ab200420; 1:1,000 dilution) (Gao et al., 2016 (link)), anti-human Caspase-1 (Santa Cruz, sc515, 1: 1,000 dilution), anti-human GSGMD (sigma, HPA044487, 1: 1,000 dilution), anti-human IL-1β (Cell signaling, #12703, 1: 1,000 dilution), anti-ASC (Santa Cruz, sc22514R, 1:1,000 dilution). Cell lysates were reprobed with a mouse monoclonal antibody anti-β-actin (clone C4, Millipore; 1:5,000 dilution).
Magnotti F., Chirita D., Dalmon S., Martin A., Bronnec P., Sousa J., Helynck O., Lee W., Kastner D.L., Chae J.J., McDermott M.F., Belot A., Popoff M., Sève P., Georgin-Lavialle S., Munier-Lehmann H., Tran T.A., De Langhe E., Wouters C., Jamilloux Y, & Henry T. (2022). Steroid hormone catabolites activate the pyrin inflammasome through a non-canonical mechanism. Cell reports, 41(2), 111472.
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5

Pyrin-ASC Inflammasome Activation

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Cells were lysed in 25mM Tris HCl, 150mM NaCl, 1mM EDTA and 0.1% NP-40 buffer containing Mini Protease Inhibitor Mixture (Roche) and sodium fluoride (Sigma) by a quick freezing and thawing step. Flag-Pyrin was immuno-precipitated using anti Flag M2 affinity gel (Sigma). ASC was cross-linked in the insoluble pellet using DSS (Disuccinimidyl suberate, ThermoFisher #21655) 2 mM (1 h at 37°C). Proteins were separated by SDS/PAGE on precast 4–15% acrylamide gels (Bio-rad) and transferred to TransBlot® Turbo™ Midi-size PVDF membranes (Bio-rad). Antibodies used were mouse monoclonal anti-FLAG® (Sigma-Aldrich, clone M2; 1:1,000 dilution), anti-Pyrin (Adipogen, AL196, 1: 1,000 dilution), anti-phospho S242 Pyrin (Abcam, ab200420; 1:1,000 dilution) (Gao et al., 2016 (link)), anti-human Caspase-1 (Santa Cruz, sc515, 1: 1,000 dilution), anti-human GSGMD (sigma, HPA044487, 1: 1,000 dilution), anti-human IL-1β (Cell signaling, #12703, 1: 1,000 dilution), anti-ASC (Santa Cruz, sc22514R, 1:1,000 dilution). Cell lysates were reprobed with a mouse monoclonal antibody anti-β-actin (clone C4, Millipore; 1:5,000 dilution).
Magnotti F., Chirita D., Dalmon S., Martin A., Bronnec P., Sousa J., Helynck O., Lee W., Kastner D.L., Chae J.J., McDermott M.F., Belot A., Popoff M., Sève P., Georgin-Lavialle S., Munier-Lehmann H., Tran T.A., De Langhe E., Wouters C., Jamilloux Y, & Henry T. (2022). Steroid hormone catabolites activate the pyrin inflammasome through a non-canonical mechanism. Cell reports, 41(2), 111472.
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