Coactosin-like Protein 1/CotL1 Antibody

COTL1 (Coactosin-like Protein) is both a cytoplasmic and plasma-appearing 15-16 kDa member of the coactosin subfamily, ADF/Actin Depolymerizing Factor family of actin-binding proteins. It is widely expressed, and found in cell types such as neutrophils, and tissues such as placenta, lung and kidney. Functionally, COTL1 interacts noncovalently with both F-actin and 5-lipoxygenase/5LO. These interactions appear to be mutually exclusive. A COTL1:F-actin interaction leads to actin binding without actin polymerization, while a 5LO:COTL1 interaction has two potential outcomes; first, 5LO sequesters COTL1, leading to a failure of actin binding, and second, COTL1 can serve as a scaffold for 5LO activity, facilitating the production of either 5HPETE or LTA4. Human COTL1 is 142 amino acids (aa) in length. It is principally composed of one ADF-H domain (aa 2-130) that possesses a utilized phosphorylation site at Ser115, and two acetylation sites at Lys102 and Lys126. COTL1 may form noncovalent homodimers and oligomers, but not when complexed to F-actin. There is one potential isoform variant that shows a 106 aa substitution for aa 1-53. Full-length human and mouse COTL1 share 95% aa sequence identity.