The CD5 molecule-like protein, also known as CD5L or CD5 antigen-like, is a member of the scavenger receptor cysteine-rich (SRCR) superfamily. This protein is expressed in various immune cells and plays a crucial role in the regulation of the immune system.
CD5L is a soluble glycoprotein that contains three SRCR domains. It is primarily expressed by macrophages in lymphoid tissues such as the spleen, lymph nodes, thymus, and bone marrow . The recombinant form of this protein, produced in HEK293 cells, consists of a single, glycosylated polypeptide chain with a calculated molecular mass of approximately 36.9 kDa .
CD5L functions as a pattern recognition molecule, binding to both lipoteichoic acid (LTA) on Gram-positive bacteria and lipopolysaccharide (LPS) on Gram-negative bacteria . This binding activity is retained in the SRCR domain 1 of CD5L. The protein plays a significant role in the innate and adaptive immune systems by recognizing and responding to microbial components.
Recombinant CD5L protein is used in various research applications, including studies on immune response, cell signaling, and disease mechanisms. The protein’s ability to bind to microbial components makes it a valuable tool for investigating host-pathogen interactions and the immune system’s response to infections.
The recombinant human CD5L protein is produced in HEK293 cells and purified to a high degree of purity, typically greater than 95% as determined by SDS-PAGE and SEC-HPLC . The protein is lyophilized from a sterile PBS solution and can be reconstituted for use in various experimental applications. It is recommended to store the protein under sterile conditions at -20°C to -80°C to maintain its stability and avoid repeated freeze-thaw cycles .