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Calmodulin

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Calmodulin is a calcium-binding protein that plays a crucial role in the regulation of various cellular processes. It functions as a calcium sensor and mediator, transducing changes in calcium levels into specific cellular responses.

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Lab products found in correlation

Calcineurin, by Enzo Life Sciences (2 mentions) Anti p ser 14 3 3 binding motif10, by Cell Signaling Technology (2 mentions) Anti p ser142 tfeb9, by Cell Signaling Technology (2 mentions) γ 32p atp, by PerkinElmer (1 mentions) Bis tris plus gel, by Thermo Fisher Scientific (1 mentions) Lithium dodecyl sulfate (lds), by Thermo Fisher Scientific (1 mentions) Pageblue protein staining solution, by Thermo Fisher Scientific (1 mentions) Dithiothreitol (dtt), by Euromedex (1 mentions)

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Human recombinant calmodulin (2 citations)

3 protocols using calmodulin

1

Dephosphorylation of Activated TFEB

Cited 2 times
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Phosphorylated FLAG-TFEB was obtained by immunoprecipitation from fed HeLa cells. Protein-G beads containing FLAG-TFEB were incubated for 40 min at 30°C in 24 µl of corresponding phosphatase reaction buffer (20 mM HEPES, pH 7.5, 10 mM MgCl2, 2 mM DTT, protease inhibitors with 1 mM CaCl2 or 10 mM EGTA) containing purified Calcineurin (100U; ENZO Life Sciences) and Calmodulin (4 mM; ENZO Life Sciences). Samples were eluted by adding 8 µl of 4X Laemmli buffer, resolved by SDS–PAGE and analysed by immunoblotting. Antibodies anti-p-Ser 14-3-3 binding motif10 (link), anti-P-Ser142-TFEB9 (link) and TFEB (Cell Signaling Technologies) were used to detect phosphorylated and total TFEB forms, respectively.
Medina D.L., Di Paola S., Peluso I., Armani A., De Stefani D., Venditti R., Montefusco S., Scotto-Rosato A., Prezioso C., Forrester A., Settembre C., Wang W., Gao Q., Xu H., Sandri M., Rizzuto R., De Matteis M.A, & Ballabio A. (2015). Lysosomal calcium signaling regulates autophagy via calcineurin and TFEB. Nature cell biology, 17(3), 288-299.
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2

Dephosphorylation of Activated TFEB

Cited 2 times
Check if the same lab product or an alternative is used in the 5 most similar protocols
Phosphorylated FLAG-TFEB was obtained by immunoprecipitation from fed HeLa cells. Protein-G beads containing FLAG-TFEB were incubated for 40 min at 30°C in 24 µl of corresponding phosphatase reaction buffer (20 mM HEPES, pH 7.5, 10 mM MgCl2, 2 mM DTT, protease inhibitors with 1 mM CaCl2 or 10 mM EGTA) containing purified Calcineurin (100U; ENZO Life Sciences) and Calmodulin (4 mM; ENZO Life Sciences). Samples were eluted by adding 8 µl of 4X Laemmli buffer, resolved by SDS–PAGE and analysed by immunoblotting. Antibodies anti-p-Ser 14-3-3 binding motif10 (link), anti-P-Ser142-TFEB9 (link) and TFEB (Cell Signaling Technologies) were used to detect phosphorylated and total TFEB forms, respectively.
Medina D.L., Di Paola S., Peluso I., Armani A., De Stefani D., Venditti R., Montefusco S., Scotto-Rosato A., Prezioso C., Forrester A., Settembre C., Wang W., Gao Q., Xu H., Sandri M., Rizzuto R., De Matteis M.A, & Ballabio A. (2015). Lysosomal calcium signaling regulates autophagy via calcineurin and TFEB. Nature cell biology, 17(3), 288-299.
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3

NLRP3 phosphorylation by diverse kinases

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GST-NLRP3 (1 μg, Abcam) was incubated of with GST-CSNK1A1 (100 ng, Sino Biological), GST-CSNK2A1 (100 ng, Sino Biological)/GST-CSNK2B (100 ng, Creative Biomart), or 6-His-GST-CAMK2B (100 ng, Sino Biological)/Calmodulin (1 μg, Enzo) with 50 μM ATP and 4 μCi of [γ32P]-ATP (PerkinElmer) in kinase buffer (50 mM HEPES pH 7.3, 100 mM NaCl, 10 mM MgCl2, 0.05% Triton X-100, 10 mM β -glycerophosphate, 5 mM NaF) at 30 °C for 30 min in a final volume of 39 μL, supplemented with 2 mM CaCl2 for CAMK2B/Calmodulin reactions. Reactions were stopped by adding 15 μL of LDS (ThermoFisher Scientific) and 6 μL of DTT (Euromedex) 500 mM. Samples were analyzed by electrophoresis using Bolt 4–12% Bis-Tris Plus gel (ThermoFisher Scientific) followed by Coomassie blue gel staining using PageBlueTM Protein staining solution (ThermoFisher Scientific) and autoradiography.
Niu T., De Rosny C., Chautard S., Rey A., Patoli D., Groslambert M., Cosson C., Lagrange B., Zhang Z., Visvikis O., Hacot S., Hologne M., Walker O., Wong J., Wang P., Ricci R., Henry T., Boyer L., Petrilli V, & Py B.F. (2021). NLRP3 phosphorylation in its LRR domain critically regulates inflammasome assembly. Nature Communications, 12, 5862.
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