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Hai cercato: N-Carbobenzoxy-L-tyrosine


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Codice catalogo: (BOSSBS-11834R-HRP)
Fornitore: Bioss
Codice articolo fornitore: BS-11834R-HRP
Codice articolo locale: BOSSBS-11834R-HRP
Descrizione: Dyrk (for dual specificity tyrosine phosphorylation regulated kinase) is the homolog of the Drosophila mnb (minibrain) gene which is required for neurogenesis. Dyrk is a dual-specificity tyrosine kinase and serine/threonine kinase, which is itself regulated by tyrosine phosphorylation. Several mammalian Dyrk related proteins have been identified and are thought to compose a family of dual specificity protein kinases. Dyrk family members, including Dyrk1A (dual specificity tyrosine-phosphorylation-regulated kinase 1A), Dyrk1B, Dyrk1C, Dyrk2, Dyrk3, Dyrk4A and Dyrk4B, are thought to be involved in diverse cellular functions. Localized to the nucleus and highly expressed in testis, muscle and the developing nervous system, Dyrk1A, also known as MNB or MNBH, functions to phosphorylate serine, threonine and tyrosine residues on various substrates involved in signaling pathways that regulate cell proliferation. Dyrk1A is a candidate gene for learning defects that are involved in Downs syndrome (DS), suggesting a possible role for Dyrk1A in the development of DS. Four isoforms of Dyrk1A exist due to alternative splicing events.
UOM: 1 * 100 µl


Codice catalogo: (BOSSBS-5453R-CY5.5)
Fornitore: Bioss
Codice articolo fornitore: BS-5453R-CY5.5
Codice articolo locale: BOSSBS-5453R-CY5.5
Descrizione: 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


Codice catalogo: (BOSSBS-0290R-CY5.5)
Fornitore: Bioss
Codice articolo fornitore: BS-0290R-CY5.5
Codice articolo locale: BOSSBS-0290R-CY5.5
Descrizione: 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


Codice catalogo: (BOSSBS-8028R-CY3)
Fornitore: Bioss
Codice articolo fornitore: BS-8028R-CY3
Codice articolo locale: BOSSBS-8028R-CY3
Descrizione: This gene is a necessary element in receptor tyrosine kinase pathways, possibly as a tyrosine phosphorylation target. It is involved in regulation of RAF in the MAPK pathway and may also play a role in a MAPK-independent pathway. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


Codice catalogo: (BOSSBS-0290R-A750)
Fornitore: Bioss
Codice articolo fornitore: BS-0290R-A750
Codice articolo locale: BOSSBS-0290R-A750
Descrizione: 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


Codice catalogo: (BOSSBS-0290R-A647)
Fornitore: Bioss
Codice articolo fornitore: BS-0290R-A647
Codice articolo locale: BOSSBS-0290R-A647
Descrizione: 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


Fornitore: Abcam
Descrizione: Anti-Tyrosine Hydroxylase Rabbit Monoclonal Antibody [clone: EP1532Y] (Alexa Fluor® 555)

Codice catalogo: (BOSSBS-3089R-A680)
Fornitore: Bioss
Codice articolo fornitore: BS-3089R-A680
Codice articolo locale: BOSSBS-3089R-A680
Descrizione: The proto oncogene c CBL was initially identified as the cellular homologue of v CBL oncogene that induces pre B cell lymphomas and myeloid leukaemias 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


Codice catalogo: (BOSSBS-5453R-CY5)
Fornitore: Bioss
Codice articolo fornitore: BS-5453R-CY5
Codice articolo locale: BOSSBS-5453R-CY5
Descrizione: 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


Codice catalogo: (BOSSBS-0290R-CY3)
Fornitore: Bioss
Codice articolo fornitore: BS-0290R-CY3
Codice articolo locale: BOSSBS-0290R-CY3
Descrizione: 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


Codice catalogo: (BOSSBS-5453R-A647)
Fornitore: Bioss
Codice articolo fornitore: BS-5453R-A647
Codice articolo locale: BOSSBS-5453R-A647
Descrizione: 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


Codice catalogo: (BOSSBS-12916R)
Fornitore: Bioss
Codice articolo fornitore: BS-12916R
Codice articolo locale: BOSSBS-12916R
Descrizione: 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


Codice catalogo: (BOSSBS-12914R-CY5)
Fornitore: Bioss
Codice articolo fornitore: BS-12914R-CY5
Codice articolo locale: BOSSBS-12914R-CY5
Descrizione: 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


Codice catalogo: (BOSSBS-1738R-CY5)
Fornitore: Bioss
Codice articolo fornitore: BS-1738R-CY5
Codice articolo locale: BOSSBS-1738R-CY5
Descrizione: 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


Codice catalogo: (BOSSBS-12915R-A647)
Fornitore: Bioss
Codice articolo fornitore: BS-12915R-A647
Codice articolo locale: BOSSBS-12915R-A647
Descrizione: 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


Codice catalogo: (BOSSBS-12916R-A488)
Fornitore: Bioss
Codice articolo fornitore: BS-12916R-A488
Codice articolo locale: BOSSBS-12916R-A488
Descrizione: 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


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