Kinase Activity Screening Analyzer ProAugust 11, 2022
A Tool for Kinase Activity Research and Elisa in Life Science. It’s also applied in high throughput screening of drug candidates in drug discovery (Target Screening). Application: Drug Candidates Screening (New Drug Discovery); Kinase Activity Assay Kit Design / Elisa Experiment Optimizing; Protein Chip Design; Disease Diagnosis by using Molecular Marker; Protein Phosphorylation Research; Peptide Activity Research; Signal Transduction Cascade Research; For Small Molecular Compounds Inhibition Research. Kinase Screening Data Statistics: human Kinase 706; Kinase/Substrate Pair 6,583; Distinct Substrate 2,931; Distinct kinase with substrate 451; Kinase with Peptide Substrate 376; Peptide Substrate 2,909; Kinase with Acitive Site 376; Phosphorylation Site 5,508; New Kinases for Activity Assay about 300. More than 450 human kinases have substrates and up to 6,583 kinase-substrate peptide pairs for Drug Target Screening and Elisa AssayOne of the most common problems computer users encounter is that a program can’t be removed. Today let’s see how to correctly uninstall Kinase Activity Screening Analyzer Pro in Windows, and I’ll also list the possible reasons that you can’t complete the removal.
Simple and Sensitive Method for Determination of Protein Kinase Activity Based on Surface Charge Change of Peptide-Modified Gold Nanoparticles As Substrates
Protein tyrosine kinases play a pivotal role in intracellular signal transduction pathways and oncogenic transformation. It is necessary to develop a simple, cost-effective, and sensitive kinase assay for study of protein kinases and discovery of kinase-target drugs. In this paper, we present a simple and sensitive method for homogeneous detection of protein kinase activity and screening of inhibitor by measuring surface charge change on the peptide-modified gold nanoparticles (GNPs) as kinase substrates. In this assay, Abl (Abelson murine leukemia viral oncogene) kinase was used as a model. In the presence of Abl kinase and ATP, the surface negative charge on GNPs significantly increases due to phosphorylation of the peptide-modified GNPs. The surface charge on the peptide-modified GNPs was measured by zeta potential analyzer. Under the optimum conditions, the zeta potential on the peptide-modified GNPs was linearly dependent on Abl kinase concentration, the linear range was from 1 to 40 nM and the detection limit was 1 nM. This method was used to evaluate the inhibition efficiency of inhibitors, and the obtained IC50 values were well in agreement with the results reported in the references. Furthermore, this method was successfully applied to determine Abl kinase activity in the cell lysates. Compared to current methods, this new method shows simplicity, short analysis time, high sensitivity, and will become a promising platform for kinase-related fundamental research and inhibitor screening.
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