Notes: This study investigated the role of the P. gingivalis haloacid dehalogenase (HAD) family phosphoserine phosphatase SerB563 during invasion of gingival epithelial cells. The Serine/Threonine Phosphatase Assay System was used to assess the activity of wildtype and mutant SerB563. (3488)

Notes: This study investigated the regulation of human Securin activity and expression. The Serine/Threonine Phosphatase Assay System was used to determine whether PP2A associated with Securin was active. Human Securin was immunoprecipitated from HCT116 cells and PP2A activity measured. This activity was compared to mock preimmune serum from HCT116 cells. The study found increased PP2A activity in the anti-human Securin cell lysates. (3487)

Notes: This study investigated the role of the dual-specificity protein phosphatase, Viral Protein 2 (VP2) from chicken anemia virus in virus-induced immunosuppression. Mutations were introduced into the VP2 sequence by overlap-expression PCR. Serine/Threonine phosphatase activity of VP2 mutants was investigated using the Serine/Threonine Phosphatase Assay System. (3525)

Notes: Purified GST-CNA-1 and GST-CNB-1 fusion proteins created from C. Elegans cna-1 and cnb-1 cDNA, two genes whose products resemble insect and mammalian calcineurin, were tested in the Serine/Threonine Phosphatase Assay System. Sixteen picomoles of each purified fusion protein were used per reaction. Data were expressed as pmol phosphate release/min/μg protein. The reactions were also incubated with 0.2mM EGTA or 1μM each of cyclosporin A and bovine cyclophilin to show specific inhibition of gene product activity. (2754)

Notes: The Serine/Threonine Phosphatase Assay System was used to determine whether the oligomerization of SpoIIE affects its phosphatase activity. The substrate used was SpoIIAA-P. (2211)

Notes: The Serine-Threonine Phosphatase Assay System was used to monitor dephosphorylation of two phosphopeptides derived from the SCR homeodomain. Dephosphorylation was performed using the catalytic subunit of the PP2A protein. Authors also used pSI for cloning, protein kinase A enzyme, PKA and PKC assays using biotinylated peptides (SignaTECT® Protein Kinase assay systems), anti-β-galactosidase for Drosophila embryo staining, and TNT® Quick Coupled Transcription/Translation systems to produce mutant and wild type protein for gel shifts. (2150)

Notes: Extracts were made from Rat-1 fibroblasts with or without IL-6 treatment. Lysates were prepared with Dignam C buffer minus the phosphatase inhibitors. The extracts were run over a G-25 spin column to remove free phosphate and were then assayed using the Serine/Threonine Phosphatase Assay System. Western Blue^® Stabilized Substrate for Alkaline Phosphatase was used for developing Western blots. (0350)

Notes: The Serine/Threonine Phosphatase Assay System was used to quantify protein phosphatase 2A levels in nuclear extracts of ECV-304 cells, a spontaneously transformed HUVEC cell line. Ten micrograms of extract were incubated with the peptide for 30min at 30°C in the recommended buffer. (1304)

Notes: The Serine/Threoine Phosphatase Assay System was used to determine phosphatase activity in cytoplasmic and membrane fractions of control and dexamethasone-treated AtT20 D16:16 mouse anterior pituitary cells. The paper contains good details of how the extracts were prepared and treated prior to the assay. Greater than 80% of the phosphatase activity was inhibited by 10nM Okadaic Acid indicating a high amount of Protein Phosphatase 2A. (0266)

Notes: The Serine/Threonine Phosphatase Assay System was used to assess protein phosphatase 2A, 2B and 2C activity in nuclear extracts of Human umbilical vein cells (HUVEC) with or without lysophosphatidylcholine treatment. Gel shifts were also performed with nuclear extracts prepared from the HUVEC cells using the SP1 Consensus Oligonucleotide. Luciferase reporter studies were also performed in HUVEC cells using pGL3 Basic-derived vectors and the Luciferase Assay System. (1305)

Notes: The Serine/Threonine Phosphatase Assay System was used to assay total cell extracts prepared from primary rat hepatocytes. A lot of detail on extract preparation is provided. (0405)