Flightless-1 Antibody recognizes endogenous levels of total Flightless-I protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human Flightless-I protein. Antibodies are purified by protein A and peptide affinity chromatography.
原厂资料：
Specificity / Sensitivity
Flightless-1 Antibody recognizes endogenous levels of total Flightless-I protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human Flightless-I protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Theflightless-I(fliI) gene was first identified inDrosophilamutant screens for genes involved in flight behavior. Homozygous mutant alleles at thefliIlocus are embryonic lethal, whereas heterozygous mutations yield a "flightless" phenotype resulting from defects in flight muscle fiber development (1). The encoded protein (flightless-I, FLII) is a highly conserved member of the gelsolin superfamily, defined by the presence of C-terminal gelsolin motifs that function as actin-binding domains (2). Genetic knock-out studies in mice and worms confirmed that Flightless-I plays a critical and highly conserved role in embryonic development, likely through its effects on actin remodeling of the cytoskeleton (3,4). Postnatally, Flightless-I is recognized to play an important role in wound repair (5). Flightless-I protein levels are increased in many wound types, and depletion of Flightless-I protein levels has been shown to accelerate wound repair by promoting fibroblast proliferation and epithelial migration (6-8). Studies in animal models suggest that Flightless-I may inhibit the wound repair process by modulating TGF-β signaling dynamics in the wound environment (9).
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