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FLII encodes a protein with a gelsolin-like actin binding domain and an N-terminal leucine-rich repeat-protein protein interaction domain. Additionally we are shipping Flightless I Homolog (Drosophila) Proteins (7) and Flightless I Homolog (Drosophila) Kits (4) and many more products for this protein.
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Chicken Polyclonal FLII Primary Antibody for WB - ABIN2785799
Olsen, Blagoev, Gnad, Macek, Kumar, Mortensen, Mann: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. in Cell 2006
Embryos defective in flightless I homolog (flii), which encodes for an actin-regulating protein, exhibit normal coilings at 24 hours post fertilization (hpf) that is followed by significantly slower burst swimming at 48 hpf.
Studies suggest that Flii enhances cutaneous squamous cell carcinoma progression by decreasing apoptosis and enhancing tumor cell invasion.
FLII plays a tumor-suppressive role and serves as a crucial determinant of resistance of prostate cancer to endocrine therapies.
These data suggest FLII as a key regulator of ERalpha-mediated transcription through its role in regulating chromatin accessibility for the binding of RNA Polymerase II and possibly other transcriptional coactivators.
Flii is constitutively secreted from macrophages and fibroblasts and is present in human plasma.
The mouse (Fli1 (show FLI1 Antibodies)) and human Fli1 (show FLI1 Antibodies) genes are similarly regulated by Ets (show ETS1 Antibodies) factors in T cells.
Fli-I promotes the GTP-bound active Rho-mediated relief of the autoinhibition of Daam1 and mDia1. Thus, Fli-I is a novel positive regulator of Rho-induced linear actin assembly mediated by DRFs.
These data suggest that Flightless-I may facilitate interaction of the p160 coactivator complex with other coactivators or coactivator complexes containing actin or actin-like proteins.
The gene that was most reproducibly up-regulated by EWS (show EWSR1 Antibodies)/FLI was NR0B1 (show NR0B1 Antibodies).
effect of FliI protein on actin remodelling is a vital part of cellular motility, contraction and adhesion. Exact signaling pathways and mechanisms underpinning FliI effects in wound healing are yet to be fully identified[review]
These findings support a novel mechanism whereby cytosolic CaMK-II influences beta-catenin dependent gene expression through Fli-I.
P-Rex1 stimulates migration through enhancing the interaction between Rac1 and the actin-remodelling protein.
Genes downstream from Flii, including TGF-beta1 (show TGFB1 Antibodies) and TGF-beta3 (show TGFB3 Antibodies), showed significantly altered expression confirming a functional effect of the Rhodamine-Flii small interfering RNA on gene expression
FliI interacts with NMMIIA to promote cell extension formation, which enables collagen remodeling in fibroblasts.
FLII functions in PPARgamma (show PPARG Antibodies) activation as a molecular switch to repress transcriptional activity by interrupting formation of the PPARgamma (show PPARG Antibodies)/RXRalpha (show RXRA Antibodies) complex.
LRRFIP2 (show LRRFIP2 Antibodies) inhibits NLRP3 (show NLRP3 Antibodies) inflammasome activation by recruiting the caspase-1 (show CASP1 Antibodies) inhibitor Flightless-I, thus outlining a new mechanism for negative regulation of NLRP3 (show NLRP3 Antibodies) inflammasome.
increasing the level of Flii in diabetic mouse wounds led to increased TLR4 (show TLR4 Antibodies) and NF- kappa B (show NFKB1 Antibodies) production. Treatment of murine diabetic wounds with neutralising antibodies to Flii led to an improvement in healing with decreased expression of TLR4 (show TLR4 Antibodies)
Using a mouse model of epidermolysis bullosa acquisita, the effect of "mopping up" Flii using Flii-neutralizing antibodies before, during, and after blister formation was determined.
FliI regulates cell migration through its localization to focal adhesions and its ability to cap actin filaments, which collectively affect focal adhesion maturation.
fli-1 plays an important role in regulating the actin-dependent events during C. elegans development.
FLI-1 controls germ line morphogenesis and rachis organization
This gene encodes a protein with a gelsolin-like actin binding domain and an N-terminal leucine-rich repeat-protein protein interaction domain. The protein is similar to a Drosophila protein involved in early embryogenesis and the structural organization of indirect flight muscle. The gene is located within the Smith-Magenis syndrome region on chromosome 17.
flightless I homolog (Drosophila)
, flightless-I homolog
, protein flightless-1 homolog