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The protein encoded by FNBP1 is a member of the formin-binding-protein family. Zusätzlich bieten wir Ihnen Formin Binding Protein 1 Antikörper (67) und Formin Binding Protein 1 Kits (10) und viele weitere Produktgruppen zu diesem Protein an.
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Results suggest that FBP17 is highly expressed in breast cancer cells and facilitates the invasion of breast cancer cells.
FBP17 is the local activator of actin polymerization that is inhibited by PM tension in the feedback loop that regulates cell migration.
Knockdown of PSTPIP2 inmacrophages enhances the assembly of FBP17, leading to'hyperactivation' of actin nucleation at podosomes and ECM degradation.
F-BAR protein Rapostlin, whose activity is regulated by Rnd2, plays a key role in spine formation through the regulation of membrane dynamics.
Results suggest a functional link between FBP17-dependent membrane tubulation and clathrin-dependent budding. Clathrin spatially directs membrane invaginations that lead to the generation of endocytic vesicles larger than those enclosed by the coat.
co-immunoprecipitation of endogenous proteins in 293T cells confirms physiological relevance of TNKS as interaction partner of FBP17
FBP17 interacts with dynamin and regulates endocytosis by forming vesicotubular structures
Data indicate that PCH protein family members such as FBP17 couple membrane deformation to actin cytoskeleton reorganization in various cellular processes.
FBP17 is recruited to clathrin-coated pits in the late stage of endocytosis, indicating its physiological role.
N-WASP-WIP complex-mediated actin polymerization is activated by phosphatidylserine-containing membranes depending on membrane curvature in the presence of Toca-1 or FBP17 and in the absence of Cdc42 and phosphatidylinositol (4,5)-bisphosphate.
formin-binding protein 17 (FBP17) recruits WASP, WASP-interacting protein (WIP), and dynamin-2 to the plasma membrane and that this recruitment is necessary for the formation of podosomes and phagocytic cups.
Rat rapostlin protein has 93% aa identity to human FBP17.
FNBP1 family proteins (FNBP1 and TRIP10) consist of FCH, FBH and SH3 domains.
FBP17 interacts with dynamin and regulates endocytosis by forming vesicotubular structures.
The protein encoded by this gene is a member of the formin-binding-protein family. The protein contains an N-terminal Fer/Cdc42-interacting protein 4 (CIP4) homology (FCH) domain followed by a coiled-coil domain, a proline-rich motif, a second coiled-coil domain, a Rho family protein-binding domain (RBD), and a C-terminal SH3 domain. This protein binds sorting nexin 2 (SNX2), tankyrase (TNKS), and dynamin\; an interaction between this protein and formin has not been demonstrated yet in human.
formin binding protein 1
, formin-binding protein 1-like
, formin-binding protein 1
, formin-binding protein 17
, formin binding protein 17
, formin-binding protein 1 homolog