Flightless I Antibody [N3K8] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 - 1:10000 IHC1:100 - 1:250 IF1:100 - 1:250

Application
WB, IHC, IF

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
145 kDa 145 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Flightless I Antibody [N3K8] detects endogenous levels of total Flightless I protein.

Clone
N3K8

Synonym(s)
FLIL, FLII, Protein flightless-1 homolog

Background
Flightless I belongs to the gelsolin family of actin-remodeling proteins distinguished by its N-terminal leucine-rich repeat (LRR) protein-protein interaction domain and C-terminal gelsolin-like actin-binding domain lacking severing activity. The LRR domain facilitates binding to partners like LRRFIP1/2, nuclear receptors, and signaling effectors, while the gelsolin domain caps actin filament barbed ends to inhibit polymerization and modulates cofilin-mediated depolymerization. FLII sequesters nuclear β-catenin to suppress Wnt/TCF transcription, competes with Dishevelled to disrupt Wnt signaling, and interacts with MyD88 to attenuate TLR4/NLRP3 inflammasome activation via LRRFIP1/2 recruitment, dampening NF-κB and IL-1β release. In TGF-β pathways, FLII associates with c-fos/c-jun (AP-1) and nuclear Akt to fine-tune Smad signaling, while actin interactions via G-actin binding regulate Hippo-YAP/TAZ nuclear localization for proliferation/apoptosis control. Nuclear translocation enables co-activator/co-repressor roles with glucocorticoid receptors and PPARγ for gene regulation. Physiologically, FLII governs cellular motility, adhesion, proliferation, differentiation, and survival critical for embryonic development, wound re-epithelialization, and tissue homeostasis. Overexpression impairs keratinocyte migration and healing by reducing Rac1/PAK signaling, whereas knockdown accelerates closure via enhanced lamellipodia. FLII promotes EMT, invasion, and metastasis through invadopodia formation and radiation resistance in colorectal tumors; in muscular dystrophy, it destabilizes dystrophin-actin links leading to fragility.

Background

Flightless I belongs to the gelsolin family of actin-remodeling proteins distinguished by its N-terminal leucine-rich repeat (LRR) protein-protein interaction domain and C-terminal gelsolin-like actin-binding domain lacking severing activity. The LRR domain facilitates binding to partners like LRRFIP1/2, nuclear receptors, and signaling effectors, while the gelsolin domain caps actin filament barbed ends to inhibit polymerization and modulates cofilin-mediated depolymerization. FLII sequesters nuclear β-catenin to suppress Wnt/TCF transcription, competes with Dishevelled to disrupt Wnt signaling, and interacts with MyD88 to attenuate TLR4/NLRP3 inflammasome activation via LRRFIP1/2 recruitment, dampening NF-κB and IL-1β release. In TGF-β pathways, FLII associates with c-fos/c-jun (AP-1) and nuclear Akt to fine-tune Smad signaling, while actin interactions via G-actin binding regulate Hippo-YAP/TAZ nuclear localization for proliferation/apoptosis control. Nuclear translocation enables co-activator/co-repressor roles with glucocorticoid receptors and PPARγ for gene regulation. Physiologically, FLII governs cellular motility, adhesion, proliferation, differentiation, and survival critical for embryonic development, wound re-epithelialization, and tissue homeostasis. Overexpression impairs keratinocyte migration and healing by reducing Rac1/PAK signaling, whereas knockdown accelerates closure via enhanced lamellipodia. FLII promotes EMT, invasion, and metastasis through invadopodia formation and radiation resistance in colorectal tumors; in muscular dystrophy, it destabilizes dystrophin-actin links leading to fragility.

References
https://pubmed.ncbi.nlm.nih.gov/17526423/ https://pubmed.ncbi.nlm.nih.gov/33330501/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%