You Searched For: N-Boc-L-tyrosine

Catalog Number: (BOSSBS-3183R-A647)

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-0290R-CY7)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3182R-CY3)

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-3182R-CY5)

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-0290R-FITC)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5453R-A750)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-0290R-HRP)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5453R-A350)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-0290R-A555)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12915R)

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 leukemia, 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-11066R-A750)

Supplier: Bioss

Description: The downstream of kinase family (Dok-1-7) are members of a class of docking proteins that include the tyrosine kinase substrates IRS-1 and Cas, which contain multiple tyrosine residues and putative SH2 binding sites. Dok-4, Dok-5 and Dok-6 are more similar to each other than to the other Dok family members, and may constitute a subfamily of the DOK genes. Dok-5 is a tyrosine kinase substrate that enhances c-Ret-dependent activation of mitogen-activated protein kinase (MAPK). Dok-5 transcript is abundant in muscle and increases during T cell activation. Dok-5 protein undergoes tyrosine phosphorylation in response to insulin and insulin-like growth factor-1. Dok-6 is highly expressed in the developing central nervous system. It associates with Ret to transduce Ret-mediated processes such as axonal projection.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11066R-CY5)

Supplier: Bioss

Description: The downstream of kinase family (Dok-1-7) are members of a class of “docking” proteins that include the tyrosine kinase substrates IRS-1 and Cas, which contain multiple tyrosine residues and putative SH2 binding sites. Dok-4, Dok-5 and Dok-6 are more similar to each other than to the other Dok family members, and may constitute a subfamily of the DOK genes. Dok-5 is a tyrosine kinase substrate that enhances c-Ret-dependent activation of mitogen-activated protein kinase (MAPK). Dok-5 transcript is abundant in muscle and increases during T cell activation. Dok-5 protein undergoes tyrosine phosphorylation in response to insulin and insulin-like growth factor-1. Dok-6 is highly expressed in the developing central nervous system. It associates with Ret to transduce Ret-mediated processes such as axonal projection.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13667R-CY3)

Supplier: Bioss

Description: Protein kinases comprise a large group of encoded factors that regulate cellular processes by catalyzing the transfer of a phosphate group to a hydroxyl acceptor in serine, threonine or tyrosine residues (1,2). Kinases are capable of influencing the oncogenic potential of cell sytems at the level of oncoprotein or tumor suppressor protein phosphorylation states (1,2). STAP-2 is a protein that contains a pleckstrin homology (PH) domain and an SH2 domain, and associates with BRK (3). BRK (breast tumor kinase, Sik) is a 451 amino acid, nonreceptor protein-tyrosine kinase that is overexpressed in breast tumors and metastatic melanoma cell lines (4). Similar to the Src family of intracellular kinses, BRK is comprised of an SH3 domain, an SH2 domain, and a catalytic domain (5). STAP-2 is susceptiple to tyrosine phosphorylation and may be invovled in tyrosine kinase-mediated signaling cascades, whose aberrant function may lead to metastis (3).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3089R-A647)

Supplier: Bioss

Description: The proto oncogene c CBL was initially identified as the cellular homologue of v CBL oncogene that induces pre B cell lymphomas and myeloid leukemias in mice. In more recent studies CBL has been shown to be a negative regulator of tyrosine kinase signaling. The ubiquitin ligase activity of CBL leads to the degradation of tyrosine kinases, thus attenuating the signal of receptors. Targets of CBL include activated protein tyrosine kinases belonging to the Src and Syk/Zap 70 families. An additional mechanism to attenuate receptor signaling is thought to be achieved by CBL’s interaction with downstream targets of tyrosine kinases, such as PI 3K and Vav.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3089R-HRP)

Supplier: Bioss

Description: The proto oncogene c CBL was initially identified as the cellular homologue of v CBL oncogene that induces pre B cell lymphomas and myeloid leukemias in mice. In more recent studies CBL has been shown to be a negative regulator of tyrosine kinase signaling. The ubiquitin ligase activity of CBL leads to the degradation of tyrosine kinases, thus attenuating the signal of receptors. Targets of CBL include activated protein tyrosine kinases belonging to the Src and Syk/Zap 70 families. An additional mechanism to attenuate receptor signaling is thought to be achieved by CBL’s interaction with downstream targets of tyrosine kinases, such as PI 3K and Vav.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-15500R-A750)

Supplier: Bioss

Description: LTK is a member of the ros/insulin receptor family of tyrosine kinases. Tyrosine-specific phosphorylation of proteins is a key to the control of diverse pathways leading to cell growth and differentiation. Multiple transcript variants encoding different isoforms have been found for this gene.

UOM: 1 * 100 µl