You Searched For: O-Benzyl-L-tyrosine

Catalog Number: (89357-406)

Supplier: Genetex

Description: Tubulin is the major building block of microtubules. This intracellular cylindrical filamentous structure is present in almost all eukaryotic cells. Microtubules function as structural and mobility elements in mitosis, intracellular transport, flagellar movement, and in the cytoskeleton. Tubulin is a heterodimer which consists of alpha tubulin and beta tubulin; both subunits have a molecular weight of 55 kDa and share considerable homology. The most widely studied tubulins have been isolated from vertebrate brains. The microtubules can be viewed in immunofluorescent microscopy allowing for the observation of the intracellular organization of proteins that are in the form of a supramolecular structure. Distinct classes of interphase microtubules have been described in tissue culture cells. They contain post translationally modified subunits of tubulin, detyrosinated alpha tubulin (Glutubulin) or acetylated alpha tubulin. The dynamic properties of microtubules of the Tyrtubulin type studied in living cells have suggested that they turnover and grow very rapidly in vivo with most microtubules exchanging within a half-time of approximately 10 minutes. Minor subpopulations of interphase microtubules have been found to be more stable in that they resist exchange for several hours, or that they are less sensitive to microtubule disrupting drugs. The coding portion of genes encoding alpha tubulin terminates in a tyrosine codon indicating that the primary gene product is tyrosinated (Tyr-Tu). Tubulin tyrosinylation is involved in the assembly status of tubulin. A specific tubulinyl tyrosine carboxypeptidase removes the terminal tyrosine to yield an alpha tubulin terminating in a glutamic acid residue while another enzyme modifies the alpha tubulin by addition of tyrosine to the carboxy terminus to offer a potential cycle of tyrosine addition and loss.

Catalog Number: (89318-790)

Supplier: Genetex

Description: Rabbit Polyclonal antibody to DYRK1B (dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1B)

Catalog Number: (10073-240)

Supplier: Prosci

Description: FER (fer tyrosine kinase) is a member of the FPS/FES family of nontransmembrane receptor tyrosine kinases, which shares a functional domain and is involved in signaling pathways through receptor tyrosine kinases (RTK) and cytokine receptors. The Fes /Fps family is distinct from c-Src, c-Abl and related nRTKs and was originally distinguished as a homolog to retroviral oncoproteins. In vivo, Fer kinase assembles into homotrimers via conserved coiled-coil domains. The N-terminal coiled-coil domains of Fer can autophosphorylate in trans, thereby regulating their cellular function through differential phosphorylation states. Growth factor exposure can induce tyrosine phosphorylation of Fer and recruitment of Fer to RTK complexes containing p85. It is expressed predominantly in mature hematopoietic cells of the granulocytic and monocytic lineage, and has been shown to be expressed in vascular endothelial cells. Fer is implicated in insulin signaling, cell-cell signaling, human prostatic proliferative diseases, and is involved in the regulation of G1 progression.

Catalog Number: (10352-108)

Supplier: Bioss

Description: Brutons tyrosine kinase (BTK) is a member of the BTK/Tec family of cytoplasmic tyrosine kinases. Like other BTK family members, it contains a pleckstrin homology (PH) domain, Src homology SH3 and SH2 domains. BTK plays an important role in B cell development. Activation of B cells by various ligands is accompanied by BTK membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate. The membrane located BTK is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinase, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation. The activation of BTK is negatively regulated by PKC beta through phosphorylation of BTK at Ser180, which results in reduced membrane recruitment, transphosphorylation and subsequent activation. The PKC/BTK inhibitory signal is likely to be a key determinant of the B cell receptor signaling threshold to maintain optimal BTK activity.

Catalog Number: (10368-554)

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.

Catalog Number: (10791-912)

Supplier: Genetex

Description: Rabbit polyclonal antibody to Receptor tyrosine kinase

Catalog Number: (10457-668)

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].

Catalog Number: (10368-612)

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.

Catalog Number: (10368-564)

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.

Catalog Number: (10374-124)

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.

Catalog Number: (10410-202)

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.

Catalog Number: (10165-854)

Supplier: Genetex

Description: Rabbit Polyclonal antibody to TrkC (neurotrophic tyrosine kinase, receptor, type 3)

Catalog Number: (76118-986)

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.

Catalog Number: (76117-364)

Supplier: Bioss

Description: The protein encoded by this gene catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The encoded protein is a type II integral membrane protein found in the Golgi body. Two transcript variants encoding the same protein have been found for this gene.

Catalog Number: (10352-106)

Supplier: Bioss

Description: Brutons tyrosine kinase (BTK) is a member of the BTK/Tec family of cytoplasmic tyrosine kinases. Like other BTK family members, it contains a pleckstrin homology (PH) domain, Src homology SH3 and SH2 domains. BTK plays an important role in B cell development. Activation of B cells by various ligands is accompanied by BTK membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate. The membrane located BTK is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinase, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation. The activation of BTK is negatively regulated by PKC beta through phosphorylation of BTK at Ser180, which results in reduced membrane recruitment, transphosphorylation and subsequent activation. The PKC/BTK inhibitory signal is likely to be a key determinant of the B cell receptor signaling threshold to maintain optimal BTK activity.

Catalog Number: (10352-110)

Supplier: Bioss

Description: Brutons tyrosine kinase (BTK) is a member of the BTK/Tec family of cytoplasmic tyrosine kinases. Like other BTK family members, it contains a pleckstrin homology (PH) domain, Src homology SH3 and SH2 domains. BTK plays an important role in B cell development. Activation of B cells by various ligands is accompanied by BTK membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate. The membrane located BTK is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinase, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation. The activation of BTK is negatively regulated by PKC beta through phosphorylation of BTK at Ser180, which results in reduced membrane recruitment, transphosphorylation and subsequent activation. The PKC/BTK inhibitory signal is likely to be a key determinant of the B cell receptor signaling threshold to maintain optimal BTK activity.