MGSSHHHHHH SSGLVPRGSH MATKIDKEAC RAAYNLVRDD GSAVIWVTFK YDGSTIVPGE QGAEYQHFIQ QCTDDVRLFA FVRFTTGDAM SKRSKFALIT WIGENVSGLQ RAKTGTDKTL VKEVVQNFAK EFVISDRKEL EEDFIKSELK KAGGANYDAQ TE.
Coactosin-Like 1 acts as a chaperone for the enzyme 5-lipoxygenase (ALOX5), which is involved in the biosynthesis of leukotrienes . Leukotrienes are lipid mediators that play a significant role in inflammatory responses. By stabilizing and influencing the activity of ALOX5, COTL1 indirectly contributes to the regulation of inflammation .
Additionally, COTL1 binds to F-actin but does not directly affect actin depolymerization . This binding is crucial for maintaining the structural integrity of the actin cytoskeleton, which is vital for various cellular functions.
Recombinant human Coactosin-Like 1 protein is produced using Escherichia coli (E. coli) expression systems. The recombinant protein is typically fused to a His-tag at the N-terminus to facilitate purification using conventional chromatography techniques . This recombinant protein is used in various research applications, including studying the protein’s function and interactions.
The recombinant COTL1 protein is valuable in research focused on understanding the molecular mechanisms underlying actin cytoskeleton regulation and inflammation. It is also used in studies investigating the role of COTL1 in various diseases, providing a foundation for developing potential therapeutic strategies.