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anti-Human WIPF1 Antikörper:
anti-Mouse (Murine) WIPF1 Antikörper:
anti-Rat (Rattus) WIPF1 Antikörper:
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Human Monoclonal WIPF1 Primary Antibody für ICS - ABIN1177221
Aspenström: The verprolin family of proteins: regulators of cell morphogenesis and endocytosis. in FEBS letters 2005
Human Polyclonal WIPF1 Primary Antibody für ELISA, WB - ABIN261101
Massarwa, Carmon, Shilo, Schejter: WIP/WASp-based actin-polymerization machinery is essential for myoblast fusion in Drosophila. in Developmental cell 2007
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 (zeige BRAF Antikörper) V600E/MAPK (zeige MAPK1 Antikörper) pathway through its promoter demethylation.
WIP controls tumor growth by boosting signals that stabilize the YAP (zeige YAP1 Antikörper)/TAZ (zeige TAZ Antikörper) 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 (zeige AKT2 Antikörper) regulates WIP and controls YAP (zeige YAP1 Antikörper)/TAZ (zeige TAZ Antikörper) stability.
Knocking down WIP expression in A549 cells significantly reduced RhoA (zeige RHOA Antikörper) levels and WIP was found to interact with RhoA (zeige RHOA Antikörper) suggesting that WIP might be executing its function by regulating RhoA (zeige RHOA Antikörper).
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 (zeige NCK1 Antikörper), CrkL (zeige CRKL Antikörper) and cortactin (zeige CTTN Antikörper).
Data indicate the WASp-interacting protein (WIP)-Wiskott-Aldrich syndrome protein (WASp) interaction in the regulation of actin-dependent processes.
These experiments identify WIP as a member of a signaling cascade comprised of Abl (zeige ABL1 Antikörper) family kinases, mTORC1 and S6K (zeige RPS6KB1 Antikörper), 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 (zeige CD19 Antikörper) 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 (zeige DBNL Antikörper) in growth factor-induced dorsal ruffle formation through its interaction with WIP.
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