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Protein Tyrosine Kinase

Protein Tyrosine Kinases are enzymes that catalyze the phosphorylation of tyrosine residues in proteins, playing crucial roles in signal transduction pathways.
These enzymes are involved in a variety of cellular processes, including cell growth, differentiation, and metabolism.
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Most cited protocols related to «Protein Tyrosine Kinase»

A total of 565 genes were chosen for analysis on the basis of review of the American College of Medical Genetics and Genomics (ACMG) gene list and the medical literature1 (link)-4 and were divided into five nonoverlapping categories (Fig. 2; and Table S3 in Supplementary Appendix 1 and Table S2 in Supplementary Appendix 2, available at NEJM.org). The first category included genes that have been associated with autosomal dominant cancer-predisposition syndromes, and it consisted of 49 classical genes (including 23 genes from the ACMG gene list5 (link)) and 11 genes that have been implicated in genetic syndromes associated with RAS mutations (sometimes called RASopathies; these include the cardiofaciocutaneous syndrome, Costello’s syndrome [also called the faciocutaneoskeletal syndrome], Noonan’s syndrome, and the multiple lentigines syndrome). These 60 genes were selected because of the potential effect of germline mutations on clinical practice, including avoidance of radiation therapy, choice of surgical approach for tumor resection, donor testing and selection for hematopoietic stem-cell transplantation, possible or proven benefits of tumor surveillance and early cancer detection, and risk-reductive surgery.3 Variants detected in these 60 genes were confirmed experimentally by an independent sequencing assay (Supplementary Appendix 1).
The second category included 29 genes that have been associated with autosomal recessive cancer-predisposition syndromes, with a focus on identifying biallelic pathogenic mutations. Variants detected in the 89 genes that have been associated with autosomal dominant or autosomal recessive cancer-predisposition syndromes were reviewed by a multidisciplinary panel for classification and reporting.5 (link)-8 (link)An additional 476 genes were chosen for evaluation on the basis of their recurrent somatic mutation in cancer (http://cancer.sanger.ac.uk/cancergenome/projects/census and www.pediatriccancergenomeproject.org/site). These genes were classified into three categories: tumor-suppressor genes (58 genes),9 (link) tyrosine kinase genes (23), and other cancer genes (395). Our analyses of the genes in these three categories focused on known hotspot-activating mutations in genes encoding kinases and on truncation mutations in genes encoding tumor-suppressor proteins and in other cancer genes.
Publication 2015
Biological Assay Cardio-Facio-Cutaneous Syndrome Costello Syndrome Diploid Cell Early Detection of Cancer Gain of Function Mutation Gene, Cancer Genes Genes, vif Germ-Line Mutation Hereditary Diseases LEOPARD Syndrome Malignant Neoplasms Multiple Pterygium Syndrome, Autosomal Dominant Mutation Neoplasms Noonan Syndrome Operative Surgical Procedures Pathogenicity Phosphotransferases Protein Tyrosine Kinase Radiotherapy Susceptibility, Disease Syndrome Tissue Donors Transplantation, Hematopoietic Stem Cell Tumor Suppressor Genes Tumor Suppressor Proteins

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Publication 2022
BRAF protein, human Diploid Cell Drug Delivery Systems EZH2 protein, human FLT3 protein, human GB virus C Genes Genetic Diversity Germ-Line Mutation Germ Line KRAS protein, human Malignant Neoplasms midostaurin Neoplasms Oncogenes Pathogenicity PIK3CA protein, human Protein Tyrosine Kinase PTEN protein, human TERT protein, human Therapeutics TP53 protein, human Tumor Suppressor Genes

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Publication 2011
Arm, Upper Cloning Vectors Codon Codon, Terminator Diphtheria Toxin Embryonic Stem Cells Exons Genes Internal Ribosome Entry Sites Introns Peptide Chain Initiation, Translational Poly A Protein Tyrosine Kinase Reading Frames
Protein-tyrosine kinase assays were performed in 384-well plates using the Z’-lyte kinase assay system and Tyr2 peptide substrate (Invitrogen) as described elsewhere (19 (link)). Chemical libraries were purchased from ChemDiv, Inc. and included a kinase-directed library (2500 compounds) a phosphatase-directed library (2500 compounds) and a diversity set (5040 compounds). Library screens were conducted in 384-well plates in a final volume of 10 µl per well. Compounds were added to each well (10 µM final), followed by a preformed complex of Hck-YEEI (10 ng/well) and Nef (1:20 molar ratio) plus the substrate peptide (2 µM). Reactions were initiated by the addition of ATP (50 µM final) and incubated at room temperature for 35 min. Reactions were developed and terminated as per the manufacturer’s protocol and fluorescence ratios were calculated as described in the text and elsewhere (19 (link)).
Publication 2009
Biological Assay cDNA Library Fluorescence Molar Peptides Phosphoric Monoester Hydrolases Phosphotransferases Protein Tyrosine Kinase

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Publication 2018
Alleles Amino Acids Animals, Transgenic Arginine Kinase Artemia Bacterial Artificial Chromosomes Binding Sites Codon, Initiator Codon, Nonsense Debility DUSP6 protein, human Embryo Females FGFR1 protein, human heat-shock protein 70.1 Heat-Shock Proteins 70 Histidine Internal Ribosome Entry Sites Larva Males Missense Mutation Mutation, Nonsense Ovum Paragangliomas 4 Promega Protein Tyrosine Kinase Strains Tissue, Membrane Zebrafish

Most recents protocols related to «Protein Tyrosine Kinase»

11 host WT mice (male) ranging from 13 to 17 weeks of age were irradiated twice with 6.02 Gy in 4 h (Faxitron CP-160). 3 WT (male) and 3 Cxcl4−/− (male) graft mice were sacrificed after isoflurane narcosis. Femora and tibiae were separated from muscle tissue and cleaned. Under sterile conditions, bone marrow was flushed out with syringes using phosphate buffered saline (PBS) with 2% fetal calf serum (FCS). Erythrocytes were lysed by incubating 5 min in 1x erythrocyte lysis buffer (BD Pharm Lyse) followed by two washing steps with PBS. Cell suspension was filtered through a 40 μm cell strainer. Tyrosine kinase KIT positive (cKIT+) cells were isolated by magnetic cell separation using murine cKIT-microbeads (Miltenyi Biotech) according to the manufacturer’s instructions. WT or Cxcl4−/− cKIT+ stem cells were transplanted into the lethally irradiated host mice 2 h after the second radiation by retroorbital injection of 5 × 105 cKit+ cells per mouse (6x WT, 5x Cxcl4−/−). To protect against infections during engraftment, antibiotics (Sulfadimethoxin & Trimethoprim, 95 mg/kg BW) were added to drinking water for 21 days after transplantation. 28 days after transplantation, success of hematopoietic stem cell engraftment was checked by taking blood samples and monitoring blood count. Mice were subjected to IRI or sham surgery as described before.
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Publication 2023
Antibiotics BLOOD Bone Marrow Cells Cell Separation Electromagnetic Radiation Erythrocytes Femur Fetal Bovine Serum Infection Isoflurane Males Microspheres Mus Muscle Tissue Narcosis Operative Surgical Procedures Phosphates Protein Tyrosine Kinase Proto-Oncogene Protein c-kit Saline Solution Stem Cells Stem Cells, Hematopoietic Sterility, Reproductive Syringes Tibia Transplantation Trimethoprim
The data that support the results of this study are in the Supplementary data, including information of the allosteric proteins in the data set (Supplementary file 1); list of the Z-scores and ranking of allosteric pockets in the data set (Supplementary file 2); KeyAlloSite prediction results of AurA kinase (Supplementary file 3); list of the predicted key allo-residues in allosteric pockets (Supplementary file 4); key allo-residues predicted by KeyAlloSite with different cutoffs (Supplementary file 5); KeyAlloSite prediction results of tyrosine-protein kinase ABL1 (Supplementary file 6); the key allo-residues predicted by our method on CALB (Supplementary file 7); the confusion matrices of KeyAlloSite in different scenarios (Supplementary file 8); comparison of KeyAlloSite and SCA methods (Supplementary file 9); phylogenetic tree of androgen receptor (Figure 2—figure supplement 1); comparison of ECS between pockets when all residue pairs and partial residue pairs were used (Figure 2—figure supplement 2); difference between the EC between orthosteric and allosteric sites and the EC between two random patches (Figure 2—figure supplement 3); distribution of the ratios of the number of key allo-residues predicted by KeyAlloSite in the number of all residues in allosteric pockets when using different cutoffs in all proteins (Figure 3—figure supplement 1); examples of distributions of the statistics corresponding to significant scores obtained from the t-test (Figure 3—figure supplement 2); and random sampling of homologous sequences (Figure 3—figure supplement 3). The homologous sequences of the proteins in the data set are available in the following GitHub repository: https://github.com/huilan1210/KeyAlloSite, Xie et al., 2023 .
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Publication 2023
Amino Acid Sequence AR protein, human Dietary Supplements Homologous Sequences Phosphotransferases Proteins Protein Tyrosine Kinase
Retflox-V805A (The Jackson Laboratory, 028548) female and male mice were bred for timed pregnancy. To inhibit Ret tyrosine kinase activity, pregnant female mice were injected i.p. with NA-PP1 (Medchem express, HY-13941/CS-1804) or vehicle (cremaphor/saline/ethanol in 1:7:2 ratio) from E16.5 through E18.5 at the dose of 32.25 mg/kg, 50 mg/kg, and 62.5 mg/kg, respectively. Pups delivered spontaneously E19.5. NA-PP1 was prepared using published methods (37 (link)). Both male and female offspring were used for experiments. To delete Ret in the UB, Tet-O-Cre (103 (link)) and Hoxb7rtTA (The Jackson Laboratory, 036718) mice were crossed into Retflox-V805A mice. Tet-O-Cre;Hoxb7rtTA;Retflox-V805A mice were bred for timed pregnancy. Pregnant females were given Dox (Henry Schein, 1315046; 2 mg/mL) dissolved in drinking water beginning E15.5, E16.5, or E17.5 through delivery. Several breeders were heterozygous for Hoxb7rtTA and yielded littermate controls without Ret deletion (Tet-O-Cre; Retflox-V805A). Offspring were genotyped through Transnetyx core service. Pups with the genotype of Tet-O-Cre;Hoxb7rtTA;Ret Retflox-V805A who were exposed to Dox in utero with resultant Ret deletion in the UB were named RetUBdel.
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Publication 2023
Cardiac Arrest Deletion Mutation Ethanol Females Genotype Heterozygote Males Mice, House OAS1 protein, human Obstetric Delivery Pregnancy Pregnant Women Protein Tyrosine Kinase Saline Solution Uterus
Docking experiments for all of the scaffolds were carried out in order to comprehend the potential interaction process of the synthesized anti-cancer compounds on the HepG2 cancer cell line. The website https://www.rcsb.org was used for drawing the structures of PI3Kalpha, Akt, c-kit tyrosine kinase, human Aurora B kinase, and STAT3 from the RCSB Protein Data Bank under the PDB IDs of 4FA6, 2X39, 1T46, 4AF3, and 6NJS, respectively [36 (link),37 (link),38 (link),39 (link),47 (link)]. ChemDraw 20.1.1 was used to create and reduce the 3D SDF structures of all of the compounds, which were then transferred to MarvinSketch. Prior to docking, the target proteins’ frameworks were evaluated, and errors in amino acid structures were rectified using Molegro Virtual Docker software [48 (link)]. The grid boxs’ centers were chosen to be the co-crystallized ligands of proteins. They re-docked in order to validate the in silico process. Molegro Virtual Docker was applied to dock active chemicals 10 times to the target proteins’ receptors. The sequences with the lowest interaction affinity and excellent connections with the targets were separated for further detailed analysis. The molecular bindings between the target and new derivatives were visualized in 2D using Discovery Studio Visualizer Software 2021.
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Publication 2023
Amino Acids AURKB protein, human Cell Lines derivatives Hep G2 Cells Ligands Malignant Neoplasms PIK3CA protein, human Proteins Protein Targeting, Cellular Protein Tyrosine Kinase Proto-Oncogene Protein c-kit Rumex STAT3 Protein
We have studied in this molecular docking investigation the different activities of all phytocompounds revealed in C. europaea polyphenolic extract, including healing activity (casein kinase-1 and glycogen synthase kinase-3β), analgesic activity (cyclooxygenase-2), antileukemic activity (Tyrosine kinase), and apoptotic effect (TRADD).
The SDF format of phenolic compounds identified in the polyphenolic extract of C. europaea and molecules used as a positive control was retrieved from the PubChem database. Then, they were prepared for molecular docking using the OPLS3 force field and the LigPrep tool in the Maestro 11.5 release of the Schrödinger Software. In all, 32 stereoisomers were generated for each ligand, taking into account ionization states at pH 7.0 and 2.0.
The crystal structures of CK1, GSK3, cyclooxygenase-2, tyrosine kinase, and TRADD were obtained from the Protein Data Bank in PDB format using the designated PDB IDs: 6GZD, 1Q5K, 6COX, 1IEP, and 1F3V, respectively. The Schrödinger-Maestro v11.5 software was used to prepare and construct the structures. Selenomethionines were converted into methionines, heavy atoms were given hydrogens, and all waters were removed. Charges and bond ordering were also allocated. The maximum heavy atom RMSD (root-mean-square-deviation) was set to 0.30 during minimization using the force field OPLS3.
The process of generating the receptor grid starts by selecting any atom of the ligand, and the grid is spaced at 20 × 20 × 20 intervals. The non-cis/trans-amide bond was penalized during SP flexible ligand docking in Glide of Schrödinger (Maestro v 11.5). The partial charge cutoff and van der Waals scaling factor were set at 0.15 and 0.80, respectively. The final score, known as the glide score, was determined based on the most energy-efficient positions. The ligand’s best-docked position with the lowest glide score value was recorded for each ligand [54 (link)].
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Publication 2023
Amides Analgesics Apoptosis Cyclooxygenase-2 Glycogen Synthase Kinase 3 Glycogen Synthase Kinase 3 beta Hydrogen Kinase I, Casein Ligands Methionine Plant Roots Protein Tyrosine Kinase Selenomethionine Stereoisomers

Top products related to «Protein Tyrosine Kinase»

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The Universal Tyrosine Kinase Assay Kit is a laboratory tool designed to measure the activity of tyrosine kinases, a class of enzymes that play a crucial role in cellular signaling pathways. The kit provides a standardized and reliable method for quantifying the phosphorylation of tyrosine residues on target substrates, a key step in the activation of tyrosine kinase-mediated signaling cascades.
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The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.
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ATP is a laboratory instrument used to measure the presence and concentration of adenosine triphosphate (ATP) in various samples. ATP is a key molecule involved in energy transfer within living cells. The ATP product provides a reliable and accurate method for quantifying ATP levels, which is useful in applications such as microbial detection, cell viability assessment, and ATP-based assays.
The HTRF KinEASE tyrosine kinase assay kit is a fluorescence-based technology used to measure the activity of tyrosine kinases. It provides a sensitive and quantitative method for detecting kinase activity in a high-throughput format. The kit utilizes HTRF technology to monitor the phosphorylation of a specific substrate by the target kinase.
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The ADP-Glo kinase assay kit is a luminescent assay designed to measure ADP, a byproduct of kinase reactions. The kit includes reagents for converting ADP to ATP, which is then detected using a luciferase/luciferin reaction and luminescence measurement.
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The ADP-Glo Kinase Assay is a luminescent assay that detects adenosine diphosphate (ADP) produced by kinase reactions. The assay uses a coupled enzymatic reaction to convert ADP to adenosine triphosphate (ATP), which is then measured using a luciferase/luciferin reaction and luminescence detection.
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More about "Protein Tyrosine Kinase"

Protein tyrosine kinases (PTKs) are a family of enzymes that play a crucial role in cellular signaling pathways.
These enzymes catalyze the phosphorylation of tyrosine residues in proteins, a process that regulates a variety of cellular processes, such as cell growth, differentiation, and metabolism.
PTKs are involved in a wide range of biological functions and are implicated in the development of various diseases, including cancer, inflammation, and neurological disorders.
Researchers often utilize a universal tyrosine kinase assay kit to measure the enzymatic activity of PTKs.
This assay kit provides a convenient and reliable method for evaluating the phosphorylation of tyrosine residues.
Additionally, the RNeasy Mini Kit is commonly used to extract and purify RNA, which can be used to analyze the expression of PTK-encoding genes.
The signaling pathways mediated by PTKs often involve the utilization of ATP as a cofactor.
The ADP-Glo kinase assay kit and the HTRF KinEASE tyrosine kinase assay kit are two popular methods for measuring the activity of PTKs, as they can detect the production of ADP during the phosphorylation reaction.
Advancements in molecular biology techniques, such as the use of the MiSeq platform for DNA sequencing, have facilitated the study of PTKs at the genomic level.
The High Pure Template Preparation Kit is a useful tool for extracting high-quality DNA samples from various biological sources, enabling researchers to investigate the genetic alterations associated with PTK-related diseases.
In cell culture experiments, fetal bovine serum (FBS) is often used to supplement the growth medium, as it provides essential nutrients and growth factors that support the proliferation and survival of cells.
The Lipofectamine 2000 transfection reagent is a common tool used to introduce genetic material, such as plasmids encoding PTKs, into cell lines for functional studies.
Overall, the study of protein tyrosine kinases is a dynamic and multifaceted field of research that continues to unravel the complexities of cellular signaling and its implications in health and disease.
The availability of various analytical tools and kits has greatly facilitated the investigation of these crucial enzymes, paving the way for the development of novel therapeutic strategies and the optimization of research protocols.