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The protein encoded by CYTH1 is a member of the PSCD family.
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CYTH1 is a novel major regulator of adhesion and engraftment in human hematopoietic stem and progenitor cells through mechanisms that, at least in part, involve the activation of integrins.
FRMD4A RNAi or inhibition of cytohesins strongly upregulated secretion of endogenous tau. These results suggest that FRMD4A, a genetic risk factor for late-onset Alzheimer's disease, regulates tau secretion by activating cytohesin-Arf6 (show ARF6 ELISA Kits) signaling.
findings suggest that cytohesin-1 is a key regulator of neutrophil adhesion to endothelial cells and to components of extracellular matrix, which may influence cell emigration through its dual opposing effect on beta2 and beta1 integrin activation
involvement of cytohesin-1 in the regulation of the functional responses of human PMNs, linked, in part at least, to the activation of Arf6 (show ARF6 ELISA Kits).
Data show that CYTIP (show CYTIP ELISA Kits) and cytoadhesin-1 are upregulated during dendritic cell maturation.
findings reveal that mycobacteria promote their uptake through a process of "inside-out" signaling involving CD14, TLR2, PI3K (show PIK3CA ELISA Kits), and cytohesin-1. This converts low avidity CR3 (show ITGAM ELISA Kits) into an active receptor leading to increased bacterial internalization
demonstrate an essential role of cytohesin-1/RhoA (show RHOA ELISA Kits) during ameboid migration in the presence of integrins
Phosphorylated cytohesin-1 is able to tightly associate with the actin cytoskeleton, and is required for maximal leukocyte function antigen-1-mediated adhesion of Jurkat cells to Icam-1 (show ICAM1 ELISA Kits).
Cytohesin-1 is required for Schwann cell migration and that phosphorylation of cytohesin-1 at the Tyr (show TYR ELISA Kits)-382 position is important for migration.
Phosphorylation of cytohesin-1 by Fyn (show FYN ELISA Kits) is required for initiation of myelination and the extent of myelination during development.
The protein encoded by this gene is a member of the PSCD family. Members of this family 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 gene is highly expressed in natural killer and peripheral T cells, and regulates the adhesiveness of integrins at the plasma membrane of lymphocytes. The encoded protein is 83% homologous to that of CYTH2.
PH, SEC7 and coiled-coil domain-containing protein 1
, SEC7 homolog B2-1
, cytoadhesin 1
, homolog of secretory protein SEC7
, pleckstrin homology, Sec7 and coiled-coil domains 1
, cytohesin 2
, SEC7 homolog A
, pleckstrin homology, Sec7 and coiled/coil domains 1(cytohesin 1)
, cytohesin 1
, pleckstrin homology, Sec7 and coiled-coil domains 1(cytohesin 1)
, pleckstrin homology, Sec7 and coiled/coil domains 1