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CYTH3 encodes a member of the PSCD (pleckstrin homology, Sec7 and coiled-coil domains) family. Zusätzlich bieten wir Ihnen Cytohesin 3 Antikörper (47) und Cytohesin 3 Proteine (7) und viele weitere Produktgruppen zu diesem Protein an.
Cytohesin-3 was upregulated in hepatocellular carcinoma tissues, correlating with overall survival/relapse-free survival and tumor size/vascular invasion.
The PH domains of cytohesin 2/ARNO (zeige CYTH2 ELISA Kits) and cytohesin 3/GRP1 are responsible for the differential effects of these proteins on cell adhesion to fibronectin (zeige FN1 ELISA Kits).
incorporation of the E345K charge reversal mutation into the GRP1 PH domain enhances PI(4,5)P(2) affinity 8-fold and yields constitutive plasma membrane targeting in cells
GRP1 is a new corepressor for thyroid hormone (zeige PTH ELISA Kits) receptors, which modulates both positive and negative regulation by T3 by decreasing TR-complex formation on thyroid response elements
Mutation of a key residue (K273A) within the canonical phosphatidylinositol phosphate - binding site of Grp1 significantly reduced the free energy of phosphatidylinositol phosphate binding.
Grp1 localizes at the beta1 integrin-positive intracellular compartment, and is involved in HGF (zeige HGF ELISA Kits)-dependent Arf6 (zeige ARF6 ELISA Kits) activation, beta1 integrin recycling and tumour angiogenesis and growth in mice.
These observations suggest that Grp1 family guanine nucleotide exchange factors are autoregulated by mechanisms that depend on plasma membrane recruitment for activation.
This gene encodes a member of the PSCD (pleckstrin homology, Sec7 and coiled-coil domains) family. PSCD family members have identical structural organization that consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with phospholipids and is responsible for association of PSCDs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. This encoded protein is involved in the control of Golgi structure and function, and it may have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.
, pleckstrin homology, Sec7 and coiled-coil domains 3
, Cytohesin 3
, ARF nucleotide-binding site opener 3
, PH, SEC7 and coiled-coil domain-containing protein 3
, general receptor of phosphoinositides 1
, SEC7 homolog C
, pleckstrin homology, Sec7 and coiled/coil domains 3