Kinase Activity Screening Analyzer Pro

August 11, 2022 By 7t7exe1 0

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Kinase Activity Screening Analyzer Pro

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By BioPharm Soft

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.

Herein we describe three applications of label-free kinase profiling using a novel type of phosphate affinity polyacrylamide gel electrophoresis. The phosphate affinity site is a polyacrylamide-bound dinuclear Mn2+ complex that enables the mobility shift detection of phosphorylated proteins from their nonphosphorylated counterpart. The first application is in vitro kinase activity profiling for the analysis of varied phosphoprotein isotypes in phosphorylation status. The activity profiles of six kinds of kinases, glycogen synthase kinase-3β, cyclin-dependent kinase 5/p35, protein kinase A, mitogen-activated protein kinase (MAPK), casein kinase II, and calmodulin-dependent protein kinase II, were determined using a substrate protein, Tau, which has a number of phosphorylation sites. Each kinase demonstrated characteristic multiple electrophoresis migration bands up-shifted from the nonphosphorylated Tau due to differences in the phosphorylation sites and stoichiometry. The second application is in vivo kinase activity profiling for the analysis of protein phosphorylation involved in intracellular signal transduction. The time course changes in the epidermal growth factor-induced phosphorylation levels of Shc and MAPK in A431 cells were visualized as highly up-shifted migration bands by subsequent immunoblotting with anti-Shc and anti-MAPK antibodies. The third application is in vitro kinase inhibition profiling for the quantitative screening of kinase-specific inhibitors. The inhibition profile of a tyrosine kinase, Abl (a histidine-tagged recombinant mouse Abl kinase), was determined using the substrate Abltide-GST (a fusion protein consisting of a specific substrate peptide for Abl and glutathione S-transferase) and the approved drug Glivec (an ATP competitor). In the kinase assay, the slower migration band, monophosphorylated Abltide-GST, increased time-dependently, whereas the faster migration band, nonphosphorylated Abltide-GST, decreased. The dose-dependent inhibition of Glivec was determined by a change in the ratio of the faster and slower migration bands, which showed an IC50 value of 1.6 μm in the presence of 0.10 mm ATP.


Protein kinases are enzymes whose abundance, protein-protein interactions, and posttranslational modifications together determine net signaling activity in cells. Large-scale data on cellular kinase activity are limited, because existing assays are cumbersome, poorly sensitive, low throughput, and restricted to measuring one kinase at a time. Here, we surmount the conventional hurdles of activity measurement with a multiplexing approach that leverages the selectivity of individual kinase-substrate pairs. We demonstrate proof of concept by designing an assay that jointly measures activity of five pleiotropic signaling kinases: Akt, IκB kinase (IKK), c-jun N-terminal kinase (JNK), mitogen-activated protein kinase (MAPK)-extracellular regulated kinase kinase (MEK), and MAPK-activated protein kinase-2 (MK2). The assay operates in a 96-well format and specifically measures endogenous kinase activation with coefficients of variation less than 20%. Multiplex tracking of kinase-substrate pairs reduces input requirements by 25-fold, with ~75 µg of cellular extract sufficient for fiveplex activity profiling. We applied the assay to monitor kinase signaling during coxsackievirus B3 infection of two different host-cell types and identified multiple differences in pathway dynamics and coordination that warrant future study. Because the Akt–IKK–JNK–MEK–MK2 pathways regulate many important cellular functions, the fiveplex assay should find applications in inflammation, environmental-stress, and cancer research.


Binding assays are increasingly used as a screening method for protein kinase inhibitors; however, as yet only a weak correlation with enzymatic activity-based assays has been demonstrated. We show that the correlation between the two types of assays can be improved using more precise screening conditions. Furthermore a marked improvement in the correlation was found by using kinase constructs containing the catalytic domain in presence of additional domains or subunits.

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