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Proc. Natl. Acad. Sci. USA 103, 11027-11032. A Porphyromonas gingivalis haloacid dehalogenase family phosphatase interacts with human phosphoproteins and is important for invasion. 2006

Tribble, G.D., Mao, S., James, C.E., and Lamont, R.J.

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)

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Mol. Cell. Biol. 26, 4017-4027. Protein phosphatase 2A stabilizes human securin. 2006

Gil-Bernabé, A.M., Romero, F., Limón-Mortés, M.C., and Tortolero, M.

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)

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J. Gen. Virol. 86, 623-630. Mutation of chicken anemia virus VP2 differentially affects serine/threonine and tyrosine protein phosphatase activities. 2005

Peters, M.A., Jackson, D.A., Crabb, B.S. and Browning, G.F.

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)

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Endocrinology 146, 2692-2698. Src homology-2-containing protein tyrosine phosphatase-1 restrains cell proliferation in human medullary thyroid carcinoma. 2005

Zatelli, M.C., Piccin, D., Tagliati, F., Bottoni, A., Luchin, A., and degli Uberti, E.C.

Notes: This paper reported on a study to determine whether protein tyrosine phosphatases (PTPs) are involved in the regulation of parafollicular C cell proliferation. The TT cell line, a thyroid medullary carcinoma cell line that contains a mutation in the RET kinase protooncogene, was used for these studies. Cell proliferation in response to treatment with somatostatin in these cells was assessed using the CellTiter® AQueous Non-Radioactive Cell Proliferation Assay. Activity of the PTP SHP-1 in response to somatostatin was measured using the Tyrosine Phosphatase Assay System. (3486)

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J. Biol. Chem. 279, 2461-2469. Reactive oxygen species mediate virus-induced STAT activation: Role of tyrosine phosphatases. 2004

Liu, T., Castro, S., Brasier, A.R., Jamaluddin, M., Garofalo, R.P. and Casola, A.

Notes: The Tyrosine Phosphatase Assay System was used to assess the level of tyrosine phosphatase activity in human alveolar type II-like epithelial cells (the A549 cell line). Cell lysates were prepared with RIPA buffer and passed over the Sephadex G25 Column provided in the kit to remove free phosphates. Three micrograms of the purified lysate were used in the assay. Viral infection of A549 cells resulted in  decreased tyrosine phosphatase activity but exposure of the cells to the antioxidant butylated hydroxyanisole (BHA) rescued tyrosine phosphatase activity. (3238)

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Biochem. Biophys. Res. Commun. 312, 531–536. Gonadotropin-releasing hormone gene products downregulate the expression of their neighboring genes that encode protein tyrosine phosphatases α and ε. 2003

Okubo, K. and Aida, K.

Notes: COS-7 cells were transiently transfected with vectors that express Protein Tyrosine Phosphatase α (PTPα) and Protein Tyrosine Phosphatase ε (PTPε) using the TransFast™ Transfection Reagent. Transfections were performed in 100mm dishes. The authors also used the Tyrosine Phosphatase Assay System to assay Tyrosine Phosphatase activity in the transfectants. For these assays, both Tyrosine Phosphopeptides were demonstrated to be substrates for PTPα and PTPε.  Data were expressed as percent of untransfected control.  (2856)

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Nature 426, 299-302. The transcription factor Eyes absent is a protein tyrosine phosphatase. 2003

Tootle, T.L., Silver, S.J., Davies, E.L., Newman, V., Latek, R.R., Mills, I.A., Selengut, J.D., Parlikar, B.E.W. and Rebay, I.

Notes: The authors used the Tyrosine Phosphatase Assay System to demonstrate that the Eyes absent (Eya) transcription factor is a tyrosine phosphatase. The researchers created Eya Domain (ED) GST-ED fusion proteins, which were then used in the Tyrosine Phosphatase Assay with various tyrosine phosphorylated substrates to determine if Eya transcription factor has tyrosine phosphatase activity. (2777)

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J. Bacteriol. 184, 577-583. Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase. 2002

Morona, J.K., Morona, R., Miller, D.C. and Paton, J.C.

Notes: After identification of the genes expressed from the Streptococcus pneumoniae Capsule locus (cps), the authors used the Tyrosine Phosphatase Assay System to further characterize the novel CpsB protein as a tyrosine phosphatase. Pneumococcal cell lysates were produced by French pressing cells in a Tris buffer. The lysates were passed over the Sephadex G25 Column supplied with the system and used directly in tyrosine phosphatase assays.  The addition of manganese was essential for active CpsB protein tyrosine phosphatase activity.  Data are expressed as pmol of free phosphate released.  (3239)

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Mol. Biol. Cell 13, 3281–3293. Calcineurin, a Calcium/Calmodulin-dependent Protein Phosphatase, Is Involved in Movement, Fertility, Egg Laying, and Growth in Caenorhabditis elegans 2002

Bandyopadhyay, J., Lee, J., Lee, J., Lee, J.I., Yu, J.R., Jee, C., Cho, J.H., Jung, S., Lee, M.H., Zannoni, S., Singson, A., Kim, D.H., Koo, H.S. and Ahnn, J.

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)

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EMBO J. 19(12), 2946-2957.

Phosphorylation status of the SCR homeodomain determines its functional activity: Essential role for protein phosphatase 2A,B'. 2000

Berry, M. and Gehring, W.

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)

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Br. J. Pharmacol. 131, 667-672. Differential role of angiotensin II receptor subtypes on endothelial superoxide formation. 2000

Sohn, H.Y., Raff, U., Hoffmann, A., Gloe, T., Heermeier, K., Galle, J. and Pohl, U.

Notes: Human umbilical veins endothelial cells (HUVEC) were treated with 100nM angiotensin II in the presence or absence of candesartan or the AT2 receptor inhibitor, PD123319. Cells were lysed with a well-described lysis buffer that included 1% Triton X-100. Five microliters of lysate was added to storage buffer containing 5µl of Tyr Phosphopeptide-2 (DADE(pY)LIPQQG) from the Tyrosine Phosphatase Assay System to assay for tyrosine phosphatase activity in the cells.  Data were normalized by protein assay and expressed as percent of a control (no treatment).  (3244)

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EMBO J. 19(7), 1467-1475. Direct interaction between the cell division protein FtsZ and the cell differentiation protein SpoIIE. 2000

Lucet, I., Feucht, A., Yudkin, M.D., Errington, J.

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)

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J. Biol. Chem. 274, 30919-30926. Interleukin-6 increases rat metalloproteinase-13 gene expression through stimulation of activator protein 1 transcription factor in cultured fibroblasts. 1999

Solis-Herruzo, J.A., Rippe, R.A., Schrum, L.W., de la Torre, P., Garcia, I., Jeffrey, J.J., Munoz-Yague, T., Brenner, D.A.

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)

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Blood 94, 2403-2413. PTPROt: An alternatively spliced and developmentally regulated B-lymphoid phosphatase that promotes G0/G1 arrest. 1999

Aguiar, R. C.T., Yakushijin, Y., Kharbanda, S., Tiwari, S., Freeman, G.J. and Shipp, M.A.

Notes: The Tyrosine Phosphatase Assay System was used to analyze E. coli expressed GST-PTPROt fusion protein. PTPROt is a putative receptor-type protein tyrosine phosphatase expressed in epithelial cells. Twenty five nanograms of glutathione column purified GST-PTPROt protein were used in the Tyrosine Phosphatase Assay.  GST tag was used as a control protein. Data are expressed as absorbance units per nanogram of protein.  (3240)

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J. Biol. Chem. 274, 34669-34675.. Transcriptional regulation of endothelial nitric-oxide synthase by an interaction between casein kinase 2 and protein phosphatase 2A. 1999

Cieslik, K., Lee, C.M., Tang, J.L., Wu, K.K.

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)

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J. Biol. Chem. 273, 21187-21193. Functional involvement of PTP-U2L in apoptosis subsequent to terminal differentiation of monoblastoid leukemia cells. 1998

Seimiya, H., Tsuruo, T.

Notes: U937 human monoblastoid leukemia cell extracts were incubated with an anti-Protein Tyrosine Phosphatase U2 antibody and protein A sepharose. The immunocomplex was washed extensively with a tyrosine phosphatase assay buffer (25mM HEPES (pH 6.0), 5mM EDTA, 10mM 2,3-dihydroxybutane-1,4-dithiol). The phosphatase activity in the immune complex was assayed using the Tyrosine Phosphatase Assay System. The PTP-U2 was more active toward PS1 than PS2 from the assay system but showed activity to both. (0421)

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J. Biol. Chem. 273, 13531-13536. Glucocorticoid regulation of calcium-activated potassium channels mediated by serine/threonine protein phosphatase 1998

Tian, L., Knaus, H.-G., Shipston, M.J.

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)

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J. Biol. Chem. 273, 14309-14314. RNA molecules that bind to and inhibit the active site of a tyrosine phosphatase. 1998

Bell, S.D., Denu, J.M., Dixon, J.E. and Ellington, A.D.

Notes: The Tyrosine Phosphatase Assay System was used to monitor inhibition of the tyrosine phosphatase Yop51 by RNA aptamers. Various concentrations of the RNA aptamers were tested with purified Yop51. The activity of the phosphatase was monitored for 6 minutes. IC50 values were obtained from the data for each aptamer. (1435)

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J. Biol. Chem. 273, 33856-33863. The second domain of the CD45 protein tyrosine phosphatase is critical for interleukin-2 secretion and substrate recruitment of TCR-zeta in vivo. 1998

Kashio, N., Matsumoto, W., Parker, S., Rothstein, D.M.

Notes: The authors used the Tyrosine Phosphatase Assay System to assay for the the protein tyrosine phosphatase (PTPase) activity of CD45 in immunoprecipitates from CD45-Jurkat cells expressing either wildtype or mutant PTPase CD45 proteins. (0918)

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J. Biol. Chem. 273, 14885-14890. Transcriptional regulation of endothelial nitric-oxide synthase by lysophosphatidylcholine 1998

Cieslik, K., Zembowicz, A., Tang, J.-L., Wu, K.K.

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)

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J. Pharmacol. Exp. Ther. 282, 1122-1129. An okadaic acid-sensitive pathway involved in the phenobarbital- mediated induction of CYP2B gene expression in primary rat hepatocyte cultures. 1997

Sidhu, J. S., Omiecinski, C. J.

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)

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