CD5L Human

The CD5 molecule-like protein, also known as CD5L, is a significant glycoprotein that plays a crucial role in the immune system. It is part of the scavenger receptor cysteine-rich (SRCR) group B family of proteins. This article delves into the background, structure, function, and applications of the human recombinant CD5L protein.

CD5L is a 50 kDa secreted glycoprotein. It is characterized by the presence of SRCR domains, which are encoded by a single exon . The protein consists of several key structural components:

• Extracellular Domain (ECD): This domain contains three SRCR domains, which are crucial for the protein’s function.
• Transmembrane Segment: A 30 amino acid segment that anchors the protein to the cell membrane.
• Cytoplasmic Domain: A 93 amino acid segment that plays a role in intracellular signaling .

CD5L is involved in various immune responses. It is known for its ability to inhibit apoptosis, particularly in macrophage cells. The protein achieves this by interacting with other molecules on the cell surface, thereby preventing programmed cell death . Additionally, CD5L has been shown to play a role in the regulation of lipid metabolism and the immune response to pathogens.

The recombinant form of CD5L is produced using advanced biotechnological methods. It is typically derived from mouse myeloma cell lines and is available in a carrier-free form to avoid interference with experimental results . The recombinant protein is used in various research applications, including:

• Cell Culture: To study the effects of CD5L on cell survival and apoptosis.
• ELISA Standards: As a standard in enzyme-linked immunosorbent assays to quantify the presence of CD5L in samples.
• Functional Studies: To investigate the role of CD5L in immune responses and lipid metabolism .