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FMNL1 encodes a formin-related protein. Zusätzlich bieten wir Ihnen Formin-Like 1 Proteine (5) und Formin-Like 1 Kits (3) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal FMNL1 Primary Antibody für ICC, IF - ABIN4312210
Gardberg, Heuser, Iljin, Kampf, Uhlen, Carpén: Characterization of Leukocyte Formin FMNL1 Expression in Human Tissues. in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society 2014
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Human Polyclonal FMNL1 Primary Antibody für IHC - ABIN966156
Olsen, Blagoev, Gnad, Macek, Kumar, Mortensen, Mann: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. in Cell 2006
Show all 3 Pubmed References
High expression of FMNL1, resulted from decreased miR-16 and/or MTA1 amplification.
FMNL1 contributes to leukemogenesis and could act in part through Rac1 regulation.
constitutively activated form of FMNL1 (FMNL1gamma) induces localization of AHNAK1 to the cell membrane.
Results suggest that macrophage coiling phagocytosis is a complex process involving several actin nucleation/regulatory factors. They also point specifically to the formins mDia1 and FMNL1 as novel regulators of spirochete uptake by human immune cells.
after Rac-dependent activation of FMNL1, srGAP2 mediates a potent mechanism to limit the duration of Rac action and inhibit formin activity during rapid actin dynamics.
Our data suggest that FRL1 is responsible for modifying actin at the macrophage podosome and may be involved in actin cytoskeleton dynamics during adhesion and migration within tissues.
Results describe N-myristoylation as a regulative mechanism of FMNL1 responsible for membrane trafficking potentially involved in a diversity of polarized processes of hematopoietic lineage-derived cells.
Western blot analysis demonstrated that the protein encoded by this gene is overexpressed in lymphoid malignancies, cancer cell lines and peripheral blood leukocyte from chronic lymphocytic leukemia (CLL) patients.
FMNL1 is required for actin assembly on lipid droplets (LDs) in vitro and for NMIIa recruitment to LDs in cells. We propose a novel acto-myosin structure regulating lipid storage: FMNL1-dependent assembly of myosin II-functionalized actin filaments on LDs facilitates their dissociation, thereby affecting LD surface-to-volume ratio and enzyme accessibility to triglycerides.
In oocyte meiosis, FMNL1 is required for spindle organization and actin assembly.
Depleting FMNL1, another Formin family member, resulted in reduced mDia1 expression, while RhoA inhibition did not alter mDia1 expression, which indicated that there was a FMNL1-mDia1-Profilin1 signaling pathway in mouse oocytes.
FMNL1 and FMNL2 are required non-redundantly in the repair of damaged myofibrils.
Binding to interphase microtubules through exon-2-encoded domain of Fmn1 provides a novel mechanism by which Fmn1 isoform Ib could coordinate actin filaments and microtubules.
the bundling activities of FRL1 and mDia2, while producing phenotypically similar bundles, differ in mechanistic detail
A new allele of limb deformity is described due to complete deletion of Fmn1, including its global control region.
In vitro rheologic assays were used to deconvolve the dynamic cross-linking activity from the bundling activity of formin FRL1 and the closely related mDia1 and mDia2.
This gene encodes a formin-related protein. Formin-related proteins have been implicated in morphogenesis, cytokinesis, and cell polarity. An alternative splice variant has been described but its full length sequence has not been determined.
, formin-like protein 1-like
, CLL-associated antigen KW-13
, formin-like protein 1
, leukocyte formin
, formin-related gene in leukocytes
, formin-related protein
, lymphocyte specific formin related protein