You Searched For: Phenyl+vinyl+sulphone

Catalog Number: (BOSSBS-12942R-A750)

Supplier: Bioss

Description: All members of the Src gene family of tyrosine kinases are characterised by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5 to 10 fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3136R-HRP)

Supplier: Bioss

Description: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5326R-A680)

Supplier: Bioss

Description: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5326R-A750)

Supplier: Bioss

Description: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-0290R-CY3)

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-CY5)

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: (BSENR-148-50)

Supplier: Biosensis

Description: Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines dopamine, epinephrine and norepinephrine. Therefore the regulation of the TH enzyme represents the central means for controlling the synthesis of these important catecholamines. FUNCTION: Plays an important role in the physiology of adrenergic neurons. CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O2 = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin. COFACTOR: Fe(2+) ion. ENZYME REGULATION: Phosphorylation leads to an increase in the catalytic activity. PATHWAY: Catecholamine biosynthesis; first step. SUBUNIT: Homotetramer. PTM: In vitro, phosphorylation of Ser-19 increases the rate of Ser-40 phosphorylation, which results in enzyme opening and activation. SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family. The presence of different DNA sequences at the TH locus confers susceptibility to various disorders of the brain including manic-depression and schizophrenia. Parkinson's disease is also considered a TH deficiency as low dopamine levels are a consistent neurochemical abnormality.

UOM: 1 * 50 µG

Catalog Number: (BOSSBS-3182R)

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-5453R-A647)

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-3183R-FITC)

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-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-13651R-CY7)

Supplier: Bioss

Description: APS (adapter molecule containing PH and SH2 domains), SH2-B and Lnk compose a family of adapter proteins, which contain a pleckstrin homology (PH) domain, an SH2 domain and a tyrosine phosphorylation site. Stimulation of B cell receptor (BCR) or T cell receptor (TCR) results in the phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of BCR, TCR and several substrates. APS, SH2-B and Lnk may bind to the ITAM domain of BCR and TCR. Lnk is tyrosine phosphorylated in response to TCR stimulation and APS has been shown to be tyrosine phosphorylated in response to BCR stimulation.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13651R-A555)

Supplier: Bioss

Description: APS (adapter molecule containing PH and SH2 domains), SH2-B and Lnk compose a family of adapter proteins, which contain a pleckstrin homology (PH) domain, an SH2 domain and a tyrosine phosphorylation site. Stimulation of B cell receptor (BCR) or T cell receptor (TCR) results in the phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of BCR, TCR and several substrates. APS, SH2-B and Lnk may bind to the ITAM domain of BCR and TCR. Lnk is tyrosine phosphorylated in response to TCR stimulation and APS has been shown to be tyrosine phosphorylated in response to BCR stimulation.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12941R)

Supplier: Bioss

Description: All members of the Src gene family of tyrosine kinases are characterized by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5- to 10-fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12942R-CY3)

Supplier: Bioss

Description: All members of the Src gene family of tyrosine kinases are characterized by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5- to 10-fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5453R-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