DLDVPIPGRFDRRVpSVAAE
DLDVPIPGRFDRRVpSVAAE (H-Asp-Leu-Asp-Val-Pro-Ile-Pro-Gly-Arg-Phe-Asp-Arg-Arg-Val-Ser(PO₃H₂)-Val-Ala-Ala-Glu-OH) is an excellent peptide substrate for calcineurin (Protein Phosphatase 2B, PP2B). The sequence is derived from the PKA regulatory subunit type II (RII) and is phosphorylated on the Ser residue. Calcineurin is a calcium-dependent, serine/threonine phosphatase that is involved in a variety of signaling pathways. Calcineurin is distinct among phosphatases because its activity requires calcium and is not sensitive to inhibition by compounds that block the related phosphatases PP1A and PP2A. The current common techniques quantify calcineurin activity by measuring released radioactive phosphate or detection of free phosphate with malachite green. Both methods involve technical challenges and have undesirable features. AAT Bioquest has developed a few excellent phosphate assays that can be used for monitoring the release of phosphate from the dephosphorylation of DLDVPIPGRFDRRVpSVAAE by calcineurin. PhosphoWorks™ Colorimetric Phosphate Assay Kit (21665) and PhosphoWorks™ Colorimetric MESG Phosphate Assay Kit (21659) can be used for the colorimetric measurement of phosphate. For higher sensitivity, the release of phosphate can be quantified fluorometrically with PhosphoWorks™ Fluorimetric Phosphate Assay Kit (21660).
References
View all 33 references: Citation Explorer
Calcineurin dephosphorylates Kelch-like 3, reversing phosphorylation by angiotensin II and regulating renal electrolyte handling.
Authors: Ishizawa, Kenichi and Wang, Qin and Li, Jinping and Yamazaki, Osamu and Tamura, Yoshifuru and Fujigaki, Yoshihide and Uchida, Shunya and Lifton, Richard P and Shibata, Shigeru
Journal: Proceedings of the National Academy of Sciences of the United States of America (2019): 3155-3160
Authors: Ishizawa, Kenichi and Wang, Qin and Li, Jinping and Yamazaki, Osamu and Tamura, Yoshifuru and Fujigaki, Yoshihide and Uchida, Shunya and Lifton, Richard P and Shibata, Shigeru
Journal: Proceedings of the National Academy of Sciences of the United States of America (2019): 3155-3160
Calcineurin controls gene transcription following stimulation of a Gαq-coupled designer receptor.
Authors: Langfermann, Daniel S and Schmidt, Tobias and Rössler, Oliver G and Thiel, Gerald
Journal: Experimental cell research (2019): 111553
Authors: Langfermann, Daniel S and Schmidt, Tobias and Rössler, Oliver G and Thiel, Gerald
Journal: Experimental cell research (2019): 111553
Calcineurin, the Ca2+-dependent phosphatase, regulates Rga2, a Cdc42 GTPase-activating protein, to modulate pheromone signaling.
Authors: Ly, Nina and Cyert, Martha S
Journal: Molecular biology of the cell (2017): 576-586
Authors: Ly, Nina and Cyert, Martha S
Journal: Molecular biology of the cell (2017): 576-586
Calcineurin Targets Involved in Stress Survival and Fungal Virulence.
Authors: Park, Hee-Soo and Chow, Eve W L and Fu, Ci and Soderblom, Erik J and Moseley, M Arthur and Heitman, Joseph and Cardenas, Maria E
Journal: PLoS pathogens (2016): e1005873
Authors: Park, Hee-Soo and Chow, Eve W L and Fu, Ci and Soderblom, Erik J and Moseley, M Arthur and Heitman, Joseph and Cardenas, Maria E
Journal: PLoS pathogens (2016): e1005873
Inhibition of calcineurin/NFAT pathway plays an essential role in renoprotective effect of tropisetron in early stage of diabetic nephropathy.
Authors: Barzegar-Fallah, Anita and Alimoradi, Houman and Razmi, Ali and Dehpour, Ahmad Reza and Asgari, Mojgan and Shafiei, Massoumeh
Journal: European journal of pharmacology (2015): 152-9
Authors: Barzegar-Fallah, Anita and Alimoradi, Houman and Razmi, Ali and Dehpour, Ahmad Reza and Asgari, Mojgan and Shafiei, Massoumeh
Journal: European journal of pharmacology (2015): 152-9
Page updated on November 3, 2024