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LC Sciences peptide microarray analysis
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JPT Peptide Technologies GmbH customized peptide microarray
Customized Peptide Microarray, supplied by JPT Peptide Technologies GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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JPT Peptide Technologies GmbH customized peptide microarrays jpt peptide
Phosphorylation of Ote at threonine 63 is critical for cell cycle progression. (A) Schematic drawing of Ote indicating the N-terminal LEM domain, the C-terminal transmembrane domain (TM), and all potential phosphorylatable residues conforming to the consensus motifs of Cdk1 (blue), Aurora-A (orange), Plk1 (green), and CK2 (red). Colored circles designate sites that were phosphorylated in vitro on peptide <t>microarrays</t> by the 4 respective recombinant kinases. (B) Immunofluorescence microscopy images showing SL2 cells stably expressing TAP-tagged wild-type Ote, a nonphosphorylatable mutant (Ote T63A), and a phosphomimetic mutant (Ote T63E) in interphase and mitosis. Ote fusion protein localization was visualized with anti-CBS (red), centrosomes were visualized with anti-γ-Tub (green), and DNA was visualized with DAPI (blue). (C) Effects on cell cycle progression in SL2 cells overexpressing wild-type and mutant Ote are shown in the graph. While wild-type Ote overexpression has no effect on the mitotic index, overexpression of the nonphosphorylatable T63A mutant leads to an increase and overexpression of the phosphomimetic T63E mutant leads to a decrease of the proportion of mitotic cells, respectively, compared to control cells overexpressing TAP-tagged EGFP. Equal expression levels of wild-type Ote, the T63A mutant, and the T63E mutant are demonstrated by Western blotting. (D) Hypothetical model demonstrating the effect of Ote phosphorylation by Aurora-A on cell cycle progression in vivo, which is derived from the results of phosphomutant studies depicted in the bottom panels.
Customized Peptide Microarrays Jpt Peptide, supplied by JPT Peptide Technologies GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/custom+peptide+microarrays/customized+peptide+microarrays+jpt+peptide/pmc03422010-153-35-37
Average 90 stars, based on 1 article reviews
customized peptide microarrays jpt peptide - by Bioz Stars, 2026-09
90/100 stars
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Image Search Results


Phosphorylation of Ote at threonine 63 is critical for cell cycle progression. (A) Schematic drawing of Ote indicating the N-terminal LEM domain, the C-terminal transmembrane domain (TM), and all potential phosphorylatable residues conforming to the consensus motifs of Cdk1 (blue), Aurora-A (orange), Plk1 (green), and CK2 (red). Colored circles designate sites that were phosphorylated in vitro on peptide microarrays by the 4 respective recombinant kinases. (B) Immunofluorescence microscopy images showing SL2 cells stably expressing TAP-tagged wild-type Ote, a nonphosphorylatable mutant (Ote T63A), and a phosphomimetic mutant (Ote T63E) in interphase and mitosis. Ote fusion protein localization was visualized with anti-CBS (red), centrosomes were visualized with anti-γ-Tub (green), and DNA was visualized with DAPI (blue). (C) Effects on cell cycle progression in SL2 cells overexpressing wild-type and mutant Ote are shown in the graph. While wild-type Ote overexpression has no effect on the mitotic index, overexpression of the nonphosphorylatable T63A mutant leads to an increase and overexpression of the phosphomimetic T63E mutant leads to a decrease of the proportion of mitotic cells, respectively, compared to control cells overexpressing TAP-tagged EGFP. Equal expression levels of wild-type Ote, the T63A mutant, and the T63E mutant are demonstrated by Western blotting. (D) Hypothetical model demonstrating the effect of Ote phosphorylation by Aurora-A on cell cycle progression in vivo, which is derived from the results of phosphomutant studies depicted in the bottom panels.

Journal: Molecular and Cellular Biology

Article Title: Functional Analysis of Centrosomal Kinase Substrates in Drosophila melanogaster Reveals a New Function of the Nuclear Envelope Component Otefin in Cell Cycle Progression

doi: 10.1128/MCB.00814-12

Figure Lengend Snippet: Phosphorylation of Ote at threonine 63 is critical for cell cycle progression. (A) Schematic drawing of Ote indicating the N-terminal LEM domain, the C-terminal transmembrane domain (TM), and all potential phosphorylatable residues conforming to the consensus motifs of Cdk1 (blue), Aurora-A (orange), Plk1 (green), and CK2 (red). Colored circles designate sites that were phosphorylated in vitro on peptide microarrays by the 4 respective recombinant kinases. (B) Immunofluorescence microscopy images showing SL2 cells stably expressing TAP-tagged wild-type Ote, a nonphosphorylatable mutant (Ote T63A), and a phosphomimetic mutant (Ote T63E) in interphase and mitosis. Ote fusion protein localization was visualized with anti-CBS (red), centrosomes were visualized with anti-γ-Tub (green), and DNA was visualized with DAPI (blue). (C) Effects on cell cycle progression in SL2 cells overexpressing wild-type and mutant Ote are shown in the graph. While wild-type Ote overexpression has no effect on the mitotic index, overexpression of the nonphosphorylatable T63A mutant leads to an increase and overexpression of the phosphomimetic T63E mutant leads to a decrease of the proportion of mitotic cells, respectively, compared to control cells overexpressing TAP-tagged EGFP. Equal expression levels of wild-type Ote, the T63A mutant, and the T63E mutant are demonstrated by Western blotting. (D) Hypothetical model demonstrating the effect of Ote phosphorylation by Aurora-A on cell cycle progression in vivo, which is derived from the results of phosphomutant studies depicted in the bottom panels.

Article Snippet: To determine whether MS-identified in vivo phosphorylation sites in the proteins Ote, spd-2, cnn, Grip75, Nup98, Grip84, Grip71, ewg, ball, qua, and CG6927 are targeted by the 4 kinases of interest, kinase profiling on customized peptide microarrays (JPT Peptide Technologies GmbH) was employed.

Techniques: Phospho-proteomics, In Vitro, Recombinant, Immunofluorescence, Microscopy, Stable Transfection, Expressing, Mutagenesis, Over Expression, Control, Western Blot, In Vivo, Derivative Assay