MOUSE ANTI TRYPANOSOMA BRUCEI PROCYCLIN PHOS. GPEET

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known as: MOUSE ANTI TRYPANOSOMA BRUCEI PROCYCLIN PHOS. GPEET
Catalog number: genta-ABS0246
Product Quantity: 0.5 ml
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Gene target: trypanosoma brucei procyclin phos gpeet

Related genes to: MOUSE ANTI TRYPANOSOMA BRUCEI PROCYCLIN PHOS. GPEET

Symbol : phoS NIH gene
LocusTag : YE4201
Synonyms : pstS
description : phosphate ABC transporter substrate-binding protein
type of gene : protein-coding
Modification date : 2015-06-26

Related Pathways to: MOUSE ANTI TRYPANOSOMA BRUCEI PROCYCLIN PHOS. GPEET

Related product to: MOUSE ANTI TRYPANOSOMA BRUCEI PROCYCLIN PHOS. GPEET

Related Articles about: MOUSE ANTI TRYPANOSOMA BRUCEI PROCYCLIN PHOS. GPEET

A Phos-tag-based micropipette-tip method for rapid and selective enrichment of phosphopeptides.

Phosphorylated peptides are attractive targets in the study of the phosphoproteome. Here, we introduce a simple and convenient micropipette-tip method for the separation of phosphorylated and nonphosphorylated peptides by using a phosphate-binding zinc(II) complex of 1,3-bis(pyridin-2-ylmethylamino)propan-2-olate (Phos-tag). A 200-μL micropipette tip containing 10 μL of swollen agarose beads functionalized with Phos-tag moieties was prepared. All steps in the phosphate-affinity separation (binding, washing, and elution) were conducted by using aqueous buffers at neutral pH values. The entire separation protocol required less than 30 min per sample. By means of three independent separation experiments, followed by mass spectrometric (MS) analyses, we identified 1,649 non-redundant phosphopeptides from the lysates of human embryonic kidney cells (the peptides sample derived from 25 μg proteins per an MS analysis). The average ratio of identified phosphopeptides to total peptides in the respective experiments was >90%, showing a high selectivity. Furthermore, the high correlation between the triplicate analyses was confirmed by scatter plots based on the normalized abundance of each peptide, as calculated by a label-free peptide relative quantification analysis in Progenesis QI. This micropipette-tip method would be thus used preferentially as an alternative to existing tools for the reliable enrichment of phosphopeptides. This article is protected by copyright. All rights reserved. - Source :PubMed

Zn(II)-Phos-Tag SDS-PAGE for Separation and Detection of a DNA Damage-Related Signaling Large Phosphoprotein.

In this chapter, we provide a standard protocol for phosphate-affinity sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Zn(2+)-Phos-tag SDS-PAGE). This technique uses a dizinc(II) complex of the phosphate-binding molecule Phos-tag in conjunction with a neutral-pH gel system, Tris [tris(hydroxymethyl)aminomethane], and acetic acid (Tris-AcOH), to detect shifts in the mobility of phosphorylated ataxia telangiectasia-mutated (ATM) kinase. This protocol, which employs a 3% (w/v) polyacrylamide gel strengthened with 0.5% (w/v) agarose, permits the separation of larger phosphoproteins with molecular masses in the order of 200 kDa over a period of approximately 4 h. Subsequently, multiple phosphorylated forms of high-molecular-mass ATM kinase (350 kDa) can be clearly detected via immunoblotting as multiple upshifted migration bands on the Zn(2+)-Phos-tag SDS-PAGE gel. The procedure described in this protocol requires a completion time of approximately 5 h from the beginning of gel preparation to the end of electrophoresis. - Source :PubMed

Development of antioxidant Pickering high internal phase emulsions (HIPEs) stabilized by protein/polysaccharide hybrid particles as potential alternative for PHOs.

We report for the first time the usage of mono-dispersed gliadin/chitosan hybrid particles as a particulate emulsifier for Pickering high internal phase emulsions (HIPEs) development. The hybrid particles with partial wettability were fabricated at pH 5.0 using a facile anti-solvent route. Stable Pickering HIPEs with internal phases of up to 83% can be prepared with low particle concentrations (0.5-2%). The hybrid latexes were effectively adsorbed and anchored at the oil-water interface to exert steric hindrance against coalescence. Concomitantly, the compressed droplets in Pickering HIPEs to form a percolating 3D-network framework endowed the emulsions viscoelastic and self-standing features. The protective effect of Pickering HIPEs on curcumin was confirmed, and the content of primary oxidation products in HIPEs was slightly lower than that in bulk oil. This work opens an attractive strategy to convert liquid oils to viscoelastic soft solids without artificial trans fats, as a potential alternative for PHOs. - Source :PubMed

Photoelectrochemical immunosensor for methylated RNA detection based on g-C3N4/CdS quantum dots heterojunction and Phos-tag-biotin.

N(6)-methyladenosine (m(6)A) is an enigmatic and abundant internal modification in eukaryotic messenger RNA (mRNA), which could affect various aspects of RNA metabolism and mRNA translation. Herein, a novel photoelectrochemical (PEC) immunosensor was constructed for m(6)A detection based on the inhibition of Cu(2+) to the photoactivity of g-C3N4/CdS quantum dots (g-C3N4/CdS) heterojunction, where g-C3N4/CdS heterojunction was used as photoactive material, anti-m(6)A antibody as recognition unit for m(6)A-containing RNA, Phos-tag-biotin as link unit and avidin functionalized CuO as PEC signal indicator. When CuO was captured on electrode through biotin-avidin affinity reaction and then treated with HCl, Cu(2+) could be released and CuxS would be formed based on the selective interaction between CdS and Cu(2+), leading the photocurrent obviously decreased. Under the optimal detection conditions, the PEC biosensor displayed a linear range of 0.01-10nM and a low detection limit of 3.53 pM for methylated RNA determination. Furthermore, the developed method could also be used to detect the expression level of m(6)A methylated RNA in serum samples of breast cancer patient before and after operative treatment. The proposed assay strategy has a great potential for detecting the expression methylation level of RNA in real sample. - Source :PubMed

Specific glutamic acid residues in targeted proteins induce exaggerated retardations in Phos-tag SDS-PAGE migration.

We describe two unique proteins, Escherichia coli ClpX and human histone H2A, that show extremely retarded migrations relative to their molecular weights in Phos-tag SDS-PAGE, despite being nonphosphorylated. Although ClpX separated into multiple migration bands in Phos-tag gels, the separation was not due to phosphorylation. The N-terminal 47-61 region of ClpX was responsible for producing multiple phosphorylation-independent structural variants, even under denaturing conditions, and some of these variants were detected as highly up-shifted bands. By systematic Ala-scanning mutation analysis in the N-47-61 region, we concluded that the Glu-51 or Glu-54 residue was responsible for the appearance of exaggerated mobility-shifting bands. Histone H2A showed a much slower migration in Phos-tag gels in comparison with other major histones having similar molecular weights, and we found that the Glu-62 or Glu-65 residue caused the retarded migration. In addition, Phos-tag SDS-PAGE permitted us to detect a shift in the mobility of the phosphorylated form of histone H2A from that of the nonphosphorylated one. This is the first report showing that exaggerated retardation in the migration of a certain protein in Phos-tag SDS-PAGE is induced by interactions between the Phos-tag molecule and the carboxylate group of a specific Glu residue on the target. - Source :PubMed

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