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anti-Human WIPF1 Antibodies:
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Human Monoclonal WIPF1 Primary Antibody for ICS - ABIN1177221
Aspenström: The verprolin family of proteins: regulators of cell morphogenesis and endocytosis. in FEBS letters 2005
Human Polyclonal WIPF1 Primary Antibody for ELISA, WB - ABIN261101
Massarwa, Carmon, Shilo, Schejter: WIP/WASp-based actin-polymerization machinery is essential for myoblast fusion in Drosophila. in Developmental cell 2007
Authors identified WIPF1 as an oncoprotein in PDAC and a direct target of miR-141/miR-200c. They also defined the miR-141/200c-WIPF1-YAP/TAZ as a novel signaling pathway that is involved in the regulation of the invasion and metastasis of human PDAC cells.
WIP deficiency should be considered as a cause for autosomal-recessive immunodeficiency
WIP residues 454-456 are the major contributor to WASp affinity, and residues 449-451 were found to have the largest effect upon WASp ubiquitylation and, presumably, degradation.
the present study identifies the WIPF1 gene as having novel oncogenic functions and playing an important role in the invasiveness and aggressiveness of thyroid cancer when aberrantly up-regulated by the BRAF V600E/MAPK pathway through its promoter demethylation.
WIP controls tumor growth by boosting signals that stabilize the YAP/TAZ complex via a mechanism mediated by the endocytic/endosomal system.
Results suggest that local invasiveness of ameloblastoma is dependent upon the migratory potential of its tumour cells as defined by their distribution of cortactin, N-WASP and WIP in correlation with F-actin cytoskeletal dynamics.
establish a new cancer stem cell signalling pathway downstream of mtp53 in which AKT2 regulates WIP and controls YAP/TAZ stability.
Knocking down WIP expression in A549 cells significantly reduced RhoA levels and WIP was found to interact with RhoA suggesting that WIP might be executing its function by regulating RhoA.
Study provides evidence that WIP and WIRE contribute to breast cancer cell invasiveness through coordinated roles. WIP seems necessary for the assembly of invasive protrusions, whereas WIRE regulates their maturation, which leads to matrix degradation.
conclude that tyrosine phosphorylation of WIP is a crucial regulator of WASP stability and function as an actin-nucleation-promoting factor
WIP was shown to interact with various binding partners, including the signaling proteins Nck, CrkL and cortactin.
Data indicate the WASp-interacting protein (WIP)-Wiskott-Aldrich syndrome protein (WASp) interaction in the regulation of actin-dependent processes.
These findings reveal WIP as a previously unreported regulator of neuronal maturation and synaptic activity
These findings indicate that WIP deficiency should be suspected in patients with features of WAS in whom WAS sequence and mRNA levels are normal.
The results suggest that some of the mutations in the WH1 domain cause the Wiskott-Aldrich syndrome syndrome in humans by perturbing the WASP-WIP complex formation.
show that the N-WASP EVH1 domain specifically binds a 25 residue motif from the WASP Interacting Protein (WIP)
X-linked thrombocytopenia caused by a mutation in the WAS gene that disrupts interaction with the (WASP)-interacting protein (WIP).
interactions of WASP and WIP are affected by two novel mutations that change the conformation of WASP and disrupt hydrogen bonding
Only in the presence of WASP-interacting protein (WIP) can human WASP suppress the growth defect of Saccharomyces cerevisiae las17Delta strain.
A 1.3 mD multiprotein complex consisting of WASp-interacting protein (WIP), Wiskott-Aldrich syndrome protein (WASp), actin, and myosin IIA formigg during NK cell activation was identified with a role in complex formation and NK cell activity regulation.
These experiments identify WIP as a member of a signaling cascade comprised of Abl family kinases, mTORC1 and S6K, which regulates neuron development and specifically, neuritic branching and complexity.
WIP is a link between membrane lipid composition and actin cytoskeleton at dendritic spines.
WIPf1 deficiency results in defective B cell function. By regulating the cortical actin cytoskeleton, WIPf1 influences the function of CD19 as a general hub for PI3K signaling.
WIP binding to actin, independently of its binding to Wiskott-Aldrich syndrome protein, is critical for the integrity of the actin cytoskeleton in T cells and for their migration into tissues.
Results show that WIP is a novel regulator of focal adhesion assembly and cell adhesion.
Data indicate the involvement of WIP (WASP Interacting Protein) in the control of migratory persistence in both mesenchymal (fibroblast) and amoeboid (B lymphocytes) motility.
Using mouse embryonic fibroblasts lacking Nck, WIP, or N-WASP, this study investigated whether an interaction of Nck with both WIP and N-WASP is required for their recruitment to vaccinia during Arp2/3-dependent actin assembly.
These data highlight similar pathogenic strategies shared by EPEC and vaccinia virus by demonstrating a requirement for both Nck and N-WASP, but not WIP or WIP family members in pathogen-induced actin assembly.
This study implicates WIP in enteropathogenic Escherichia coli-mediated actin polymerization and pedestal elongation.
These findings identify a novel role for mAbp1 in growth factor-induced dorsal ruffle formation through its interaction with WIP.
WIP participates in the actin reorganization that leads to ruffle formation.
WIP regulates FcepsilonRI-mediated mast cell activation by regulating Syk levels and actin cytoskeleton rearrangement.
results suggest that WASP and WIP are not essential for T lymphocyte rolling and adhesion, but play important and partially redundant roles in T cell chemotaxis in vitro and homing in vivo and function downstream of small GTPases
WIP acts as a negative regulator of fibroblast migration.
WASP-interacting protein stabilizes Wiskott-Aldrich syndrome protein(WASP) and suggest that it may also be important for its function
These results indicate that WIP is essential for IL-2 signaling and responsiveness in T cells, possibly because of its critical role in TCR-triggered actin cytoskeletal reorganization.
platelet-associated IgAs negatively modulate glycoprotein VI signaling and function in Wiskott-Aldrich syndrome protein-interacting protein KO mice.
This gene encodes a protein that plays an important role in the organization of the actin cytoskeleton. The encoded protein binds to a region of Wiskott-Aldrich syndrome protein that is frequently mutated in Wiskott-Aldrich syndrome, an X-linked recessive disorder. Impairment of the interaction between these two proteins may contribute to the disease. Two transcript variants encoding the same protein have been identified for this gene.
WAS/WASL interacting protein family, member 1
, WAS/WASL-interacting protein family member 1
, Wiskott-Aldrich syndrome protein interacting protein
, WASP interacting protein
, WASP-interacting protein
, protein PRPL-2
, wiskott-Aldrich syndrome protein-interacting protein