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The protein encoded by CYTIP contains 2 leucine zipper domains and a putative C-terminal nuclear targeting signal, but does not have any hydrophobic regions. De plus, nous expédions Cytohesin 1 Interacting Protein Anticorps (57) et Cytohesin 1 Interacting Protein Protéines (5) et beaucoup plus de produits pour cette protéine.
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Cytohesin-1 (Montrer CYTH1 Kits ELISA) is required for Schwann cell migration and that phosphorylation of cytohesin-1 (Montrer CYTH1 Kits ELISA) at the Tyr (Montrer TYR Kits ELISA)-382 position is important for migration.
Phosphorylation of cytohesin-1 (Montrer CYTH1 Kits ELISA) by Fyn (Montrer FYN Kits ELISA) is required for initiation of myelination and the extent of myelination during development.
Data suggest a suppressive function for Cytip in mouse dendritic cells in limiting immune responses.
These data suggest that Cybr is not absolutely required for hematopoietic cell development or function, but stem cells lacking Cybr are at a developmental disadvantage compared to wild-type cells.
Cybr represses the expression of T-bet and IFN-gamma (Montrer IFNG Kits ELISA) via an inhibition of p38 (Montrer CRK Kits ELISA) in T-cells and consequently reduces host resistance to bacterial infection in mice.
demonstrate an essential role of cytohesin-1 (Montrer CYTH1 Kits ELISA)/RhoA (Montrer RHOA Kits ELISA) during ameboid migration in the presence of integrins
CASP has a direct role in the secretion of IFN-gamma, and NK cell motility and ability to kill tumor cells. CASP polarizes to the leading edge of migrating NK cells, and to the immunological synapse when engaged with tumor cells.
a newly identified binding partner of CYTIP, SOCS-1 (Montrer SOCS1 Kits ELISA), and confirm its function in regulating the degradation of CYTIP by the proteasome
loss of DNA methylation enables HIF-driven cytohesin 1 interacting protein expression to protect cancer cells from death cytokine signals
on infection of human monocyte-derived dendritic cells with herpes simplex virus type 1 (HSV-1), CYTIP is rapidly degraded and as a consequence beta-2 integrins, predominantly LFA-1 (Montrer ITGAL Kits ELISA), are activated
observations suggest that CASP is a scaffolding protein that facilitates the function of at least one member of the cytohesin/ARNO (Montrer CYTH2 Kits ELISA) family in response to specific cellular stimuli
Cybr not only regulates lymphocyte adhesion and cell-cell interaction but also contributes to the regulation of the signaling cascade and of the genetic program downstream of the T cell receptor.
These results suggest that endosomal SNX27 may recruit CASP to orchestrate intracellular trafficking and/or signaling complexes.
The protein encoded by this gene contains 2 leucine zipper domains and a putative C-terminal nuclear targeting signal, but does not have any hydrophobic regions. This protein is expressed weakly in resting NK and T cells. The encoded protein modulates the activation of ARF genes by CYTH1. This protein interacts with CYTH1 and SNX27 proteins and may act to sequester CYTH1 protein in the cytoplasm.
, cytohesin binder and regulator
, cytohesin binding protein HE
, cytohesin-1 interacting protein
, cytohesin-associated scaffolding protein
, cytohesin-binding protein HE
, cytohesin-interacting protein
, pleckstrin homology Sec7 and coiled-coil domains-binding protein
, pleckstrin homology, Sec7 and coiled-coil domains, binding protein
, pleckstrin homology, Sec7 and coiled/coil domains, binding protein
, cytohesin binding protein
, cytohesin 1 interacting protein
, pleckstrin homology Sec7 and coiled-coil domain-binding protein
, cytohesin-interacting protein-like