You Searched For: N-Boc-L-tyrosine

Catalog Number: (BOSSBS-5175R-CY7)

Supplier: Bioss

Description: Vital cellular functions such as cell proliferation and signal transduction are regulated in part by the balance between the activities of protein tyrosine kinases (PTK) and protein tyrosine phosphatases (PTPs). The protein contains a 121 residue extracellular domain, a single transmembrane segment, and 2 tandem intracytoplasmic catalytic domains. The PTP alpha protein is ubiquitously expressed and may play a fundamental role in the physiology of all cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13675R-CY5)

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-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-5638R-CY5)

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-CY3)

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-3183R-CY7)

Supplier: Bioss

Description: Gab2 (Grb2-associated binder-2) is an adaptor protein involved in numerous intracellular signaling pathways via its interaction with receptor tyrosine kinases (RTKs), growth factors and cytokines. Gab2 is a substrate of various RTKs, including EGFR, insulin receptor, cytokine receptors as well as B and T cell antigen receptors; Gab2 acts as a docking protein for several SH2-containing proteins. Upon tyrosine phosphorylation, Gab2 interacts with SHP2 tyrosine phosphatase and GRB2 adaptor protein PI3-kinase, CrkL and SHC.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3183R-A680)

Supplier: Bioss

Description: Gab2 (Grb2-associated binder-2) is an adaptor protein involved in numerous intracellular signaling pathways via its interaction with receptor tyrosine kinases (RTKs), growth factors and cytokines. Gab2 is a substrate of various RTKs, including EGFR, insulin receptor, cytokine receptors as well as B and T cell antigen receptors; Gab2 acts as a docking protein for several SH2-containing proteins. Upon tyrosine phosphorylation, Gab2 interacts with SHP2 tyrosine phosphatase and GRB2 adaptor protein PI3-kinase, CrkL and SHC.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5175R-CY3)

Supplier: Bioss

Description: Vital cellular functions such as cell proliferation and signal transduction are regulated in part by the balance between the activities of protein tyrosine kinases (PTK) and protein tyrosine phosphatases (PTPs). The protein contains a 121 residue extracellular domain, a single transmembrane segment, and 2 tandem intracytoplasmic catalytic domains. The PTP alpha protein is ubiquitously expressed and may play a fundamental role in the physiology of all cells.

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-6914R-CY5.5)

Supplier: Bioss

Description: Tyrosine kinase of the non-receptor type. Probably performs an important function, perhaps in regulatory processes such as cell cycle control.Fer protein is a member of the FPS/FES family of nontransmembrane receptor tyrosine kinases. It regulates cell-cell adhesion and mediates signaling from the cell surface to the cytoskeleton via growth factor receptors. [provided by RefSeq, Jul 2008].

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5984R)

Supplier: Bioss

Description: ABI2 (Abelson interactor 2) belongs to the ABI family. The Abelson interactors are among a group of proteins that interact with Abl tyrosine kinase, a non-receptor tyrosine kinase whose activation results in the regulation of cytoskeleton function, cell growth and apoptosis in response to a variety of biological stimuli.

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-12144R-CY7)

Supplier: Bioss

Description: Src homology 2 (SH2) domains bind specifically to tyrosine-phosphorylated proteins that temporally participate in signal transduction events (1). 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 (2,3). Human Sck transcripts are present at high levels in liver, pancreas, prostate and ovary (4,5). In vascular endothelial cells, Sck participates in VEGF-induced signal transduction (6). 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 (7,8).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12144R-CY3)

Supplier: Bioss

Description: Src homology 2 (SH2) domains bind specifically to tyrosine-phosphorylated proteins that temporally participate in signal transduction events (1). 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 (2,3). Human Sck transcripts are present at high levels in liver, pancreas, prostate and ovary (4,5). In vascular endothelial cells, Sck participates in VEGF-induced signal transduction (6). 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 (7,8).

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

Catalog Number: (BOSSBS-3399R-CY5)

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