You Searched For: N-Boc-L-tyrosine

Catalog Number: (BOSSBS-6271R-CY7)

Supplier: Bioss

Description: Probable receptor with tyrosine-protein kinase activity; important for development.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12144R-A750)

Supplier: Bioss

Description: Src homology 2 (SH2) domains bind specifically to tyrosine-phosphorylated proteins that temporally participate in signal transduction events. Shc-like protein (Sck) is a neuronal adaptor protein that contains an N-terminal PTB (phosphotyrosine binding) domain, a collagen homology (CH) domain, and a conserved C-terminal SH2 domain. Human Sck transcripts are present at high levels in liver, pancreas, prostate and ovary. In vascular endothelial cells, Sck participates in VEGF-induced signal transduction. Treatment of human umbilical vein endothelial (HUVEC) cells with VEGF induces recruitment of Sck to tyrosine-1175 of the kinase insert domain-containing receptor (KDR) and enhances Sck tyrosine phosphorylation.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3399R)

Supplier: Bioss

Description: The steady state of protein tyrosyl phosphorylation in cells is regulated by the opposing action of tyrosine kinases and protein tyrosine phosphatases (PTPs). Several groups have independently identified a non transmembrane PTP, designated SHPTP1 (also known as PTP1C, HCP and SHP), which is primarily expressed in hematopoietic cells and characterized by the presence of two SH2 domains N terminal to the PTP domain. A second and much more widely expressed PTP with SH2 domains, SHPTP2 (also designated PTP1D and Syp), has been identified. SHP2 is a protein tyrosine phosphatase that is widely expressed and plays a regulatory role in various cell signaling events that are important for many cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3404R-CY7)

Supplier: Bioss

Description: The steady state of protein tyrosyl phosphorylation in cells is regulated by the opposing action of tyrosine kinases and protein tyrosine phosphatases (PTPs). Several groups have independently identified a non transmembrane PTP, designated SHPTP1 (also known as PTP1C, HCP and SHP), which is primarily expressed in hematopoietic cells and characterized by the presence of two SH2 domains N terminal to the PTP domain. A second and much more widely expressed PTP with SH2 domains, SHPTP2 (also designated PTP1D and Syp), has been identified. SHP2 is a protein tyrosine phosphatase that is widely expressed and plays a regulatory role in various cell signaling events that are important for many cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration.

UOM: 1 * 100 µl

Supplier: Biotium

Description: Protein phosphorylation is a fundamental event in the regulation of a large number of intracellular processes. Phosphorylation of specific tyrosine residues is the result of activation or stimulation of their respective protein tyrosine kinases. The phosphorylated proteins can be auto-phosphorylated kinases or certain cellular protein substrates. Tyrosine-phosphorylated proteins are involved in signal transduction and in the regulation of cell proliferation. Antibody to phosphotyrosine provides an excellent tool for the detection, characterization, and purification of phosphotyrosine containing proteins. This MAb shows no cross-reaction with other phosphoamino acids and is superb for multiple applications including staining of formalin/paraffin tissues.

Supplier: Biotium

Description: Protein phosphorylation is a fundamental event in the regulation of a large number of intracellular processes. Phosphorylation of specific tyrosine residues is the result of activation or stimulation of their respective protein tyrosine kinases. The phosphorylated proteins can be auto-phosphorylated kinases or certain cellular protein substrates. Tyrosine-phosphorylated proteins are involved in signal transduction and in the regulation of cell proliferation. Antibody to phosphotyrosine provides an excellent tool for the detection, characterization, and purification of phosphotyrosine containing proteins. This MAb shows no cross-reaction with other phosphoamino acids and is superb for multiple applications including staining of formalin/paraffin tissues.

Catalog Number: (BOSSBS-5400R-A750)

Supplier: Bioss

Description: c-Kit is a transmembrane tyrosine kinase encoded by the cKit proto oncogene. c-Kit acts to regulate a variety of biological responses including cell proliferation, apoptosis, chemotaxis and adhesion. Ligand binding to the extracellular domain leads to autophosphorylation on several tyrosine residues within the cytoplasmic domain, and activation. Mutations in c-Kit have been found to be important for tumor growth and progression in a variety of cancers including mast cell diseases, gastrointestinal stromal tumor, acute myeloid leukaemia, Ewing sarcoma and lung cancer. Phosphorylation at tyrosine 721 of c-Kit allows binding and activation of PI3 kinase.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13675R)

Supplier: Bioss

Description: B cell adaptor for phosphoinositide 3-kinase (BCAP) is a tyrosine kinase substrate that bridges B cell receptor (BCR) associated kinases to the PIK3 pathway. Syk, Btk or Lyn-dependent tyrosine phosphorylation of BCAP, provides binding sites for the p85 subunit of PIK3. BCAP mRNA is present in mouse spleen, thymus, liver, lung, macrophage and B cell lines. Human BCAP maps to chromosome 10q24.2.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1466R-CY5)

Supplier: Bioss

Description: Nck is a highly conserved, oncogenic protein. It is a common target for the action of different surface receptors, encoding one SH2 and three SH3 domains, the Src homology motifs found in nonreceptor tyrosine kinases, Ras GTPase activating protein, phosphatidylinositol 3 kinase, and phospholipase Cg. Nck is widely expressed in various tissues and in cell lines from human, murine, and rat origins. Nck is phosphorylated on tyrosine, serine, and threonine residues in response to stimulation of EGF and PDGF in A431 and NIH 3T3 cells respectively. Like other SH2 containing proteins, Nck is associated with tyrosine autophosphorylated EGF or PDGF receptors via its SH2 domain. Overexpression of Nck leads to transformation of NIH 3T3 cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1135R-A488)

Supplier: Bioss

Description: c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1135R-A647)

Supplier: Bioss

Description: c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1135R-CY5.5)

Supplier: Bioss

Description: c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-6850R-CY5.5)

Supplier: Bioss

Description: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-10406R-CY5)

Supplier: Bioss

Description: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3404R-CY5.5)

Supplier: Bioss

Description: The steady state of protein tyrosyl phosphorylation in cells is regulated by the opposing action of tyrosine kinases and protein tyrosine phosphatases (PTPs). Several groups have independently identified a non transmembrane PTP, designated SHPTP1 (also known as PTP1C, HCP and SHP), which is primarily expressed in hematopoietic cells and characterized by the presence of two SH2 domains N terminal to the PTP domain. A second and much more widely expressed PTP with SH2 domains, SHPTP2 (also designated PTP1D and Syp), has been identified. SHP2 is a protein tyrosine phosphatase that is widely expressed and plays a regulatory role in various cell signaling events that are important for many cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3399R-CY7)

Supplier: Bioss

Description: The steady state of protein tyrosyl phosphorylation in cells is regulated by the opposing action of tyrosine kinases and protein tyrosine phosphatases (PTPs). Several groups have independently identified a non transmembrane PTP, designated SHPTP1 (also known as PTP1C, HCP and SHP), which is primarily expressed in hematopoietic cells and characterized by the presence of two SH2 domains N terminal to the PTP domain. A second and much more widely expressed PTP with SH2 domains, SHPTP2 (also designated PTP1D and Syp), has been identified. SHP2 is a protein tyrosine phosphatase that is widely expressed and plays a regulatory role in various cell signaling events that are important for many cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration.

UOM: 1 * 100 µl