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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. De plus, nous expédions Flightless I Homolog (Drosophila) Anticorps (36) et Flightless I Homolog (Drosophila) Kits (5) et beaucoup plus de produits pour cette protéine.
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Low FLII expression is associated with lung carcinoma.
Data show that the ability of Ca(2+) to accentuate the activity of NLRP3 inflammasome is abrogated in Flightless-I (FliI) and leucine-rich repeat FliI-interaction protein 2 (LRRFIP2)-knockdown macrophages.
Together, the data demonstrate the critical requirement of GGAA-microsatellites as EWS (Montrer EWSR1 Protéines)/FLI activating response elements in vivo and reveal an unexpected role for the EWS (Montrer EWSR1 Protéines) portion of the EWS (Montrer EWSR1 Protéines)/FLI fusion in binding to sweet-spot GGAA-microsatellites.
FLII is a component of the ChREBP (Montrer MLXIPL Protéines) transcriptional complex and negatively regulates ChREBP (Montrer MLXIPL Protéines) function in cancer cells.
Demonstrate an important role for Flii in the development and regulation of the epidermal barrier, which may contribute to the impaired healing and skin fragility of epidermolysis bullosa patients.
FLII is associated with SENP3 and the MLL1/2 complex and FLII is indispensible for H3K4 methylation and proper loading of active RNA polymerase II at this gene locus.
Flightless-I (Drosophila) homolog (FLII) activates TGFbeta1 (Montrer TGFB1 Protéines)-mediated expression of COL1A2 (Montrer COL1A2 Protéines) gene.
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.
Fluorescence resonance energy transfer experiments showed that FliI-NMMIIA interactions require Ca(2 (Montrer CA2 Protéines)+) influx. We conclude that Ca(2 (Montrer CA2 Protéines)+) influx through the TRPV4 (Montrer TRPV4 Protéines) channel regulates FliI-NMMIIA interaction, which in turn enables generation of the cell extensions essential for collagen remodeling
Flii genetic expression is enhances tissue regeneration, after claw amputation.
P-Rex1 stimulates migration through enhancing the interaction between Rac1 and the actin-remodelling protein.
Genes downstream from Flii, including TGF-beta1 (Montrer TGFB1 Protéines) and TGF-beta3 (Montrer TGFB3 Protéines), 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 (Montrer PPARG Protéines) activation as a molecular switch to repress transcriptional activity by interrupting formation of the PPARgamma (Montrer PPARG Protéines)/RXRalpha (Montrer RXRA Protéines) complex.
LRRFIP2 (Montrer LRRFIP2 Protéines) inhibits NLRP3 (Montrer NLRP3 Protéines) inflammasome activation by recruiting the caspase-1 (Montrer CASP1 Protéines) inhibitor Flightless-I, thus outlining a new mechanism for negative regulation of NLRP3 (Montrer NLRP3 Protéines) inflammasome.
increasing the level of Flii in diabetic mouse wounds led to increased TLR4 (Montrer TLR4 Protéines) and NF- kappa B (Montrer NFKB1 Protéines) production. Treatment of murine diabetic wounds with neutralising antibodies to Flii led to an improvement in healing with decreased expression of TLR4 (Montrer TLR4 Protéines)
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.
These findings strongly demonstrate that the three single nucleotide polymorphisms of FLII gene could be utilized as molecular markers for future assisted selection in cattle breeding program.
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.
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.
protein flightless-1 homolog
, flightless I homolog (Drosophila)
, flightless-I homolog
, flightless I homolog