Calcyphosine-like (CAPSL) was identified as a protein expressed in various tissues, including adipose tissue. The human recombinant form of CAPSL is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain containing 228 amino acids. It has a molecular mass of approximately 26.3 kDa and includes a 20 amino acid His-Tag at the N-terminus, which aids in its purification through chromatographic techniques .
CAPSL has been implicated in several biological processes, particularly in adipogenesis and lipogenesis. Studies have shown that CAPSL is regulated in conditions such as Multiple Symmetric Lipomatosis (MSL), a rare adipose tissue disorder characterized by the disproportionate accumulation of subcutaneous adipose tissue . CAPSL’s role in adipocyte biology suggests that it may be involved in the regulation of autophagy, a process crucial for cellular homeostasis and energy balance.
Research has highlighted the potential involvement of CAPSL in various medical conditions. For instance, dysfunction of the CAPSL gene has been associated with Familial Exudative Vitreoretinopathy (FEVR), a genetic disorder affecting retinal angiogenesis. Studies have shown that CAPSL depletion in human retinal microvascular endothelial cells impairs tube formation, cell proliferation, and migration, which are critical for proper vascular development .
The recombinant form of CAPSL is used in various research applications to study its function and role in different biological processes. By producing CAPSL in a recombinant form, researchers can investigate its interactions, regulatory mechanisms, and potential therapeutic applications. The ability to produce CAPSL recombinantly also facilitates the development of diagnostic tools and treatments for conditions associated with its dysfunction.