CD5L exhibits multifaceted roles in immunity and metabolism:
Macrophage Polarization: Drives M2 macrophage polarization via autophagy and ID3 transcription factor upregulation, mirroring IL-10 effects .
Apoptosis Inhibition: Protects macrophages, T cells, and foam cells from apoptosis, particularly in atherosclerotic plaques .
Pathogen Recognition: Binds bacterial lipoteichoic acid (Gram+) and lipopolysaccharide (Gram−) .
Lipid Metabolism: Promotes fatty acid endocytosis into adipocytes via CD36, enhancing lipolysis and contributing to obesity-related inflammation .
Th17 Cell Regulation: Alters lipid content in Th17 cells, limiting RORγt activity and pro-inflammatory gene expression .
Recent studies highlight CD5L’s structural and functional complexity:
Atherosclerosis: CD5L sustains foam cell survival by inhibiting oxidized LDL-induced apoptosis, accelerating plaque formation .
Autoimmunity: Alters IgM-receptor interactions, promoting long-lived plasma cells that produce pathogenic IgG autoantibodies .
CD5L Human, HEK is produced under stringent conditions:
Parameter | Specification |
---|---|
Purity | >95% (SDS-PAGE) |
Endotoxin Levels | <0.1 EU/µg |
Formulation | Lyophilized from PBS (pH 7.5), reconstituted to 0.5 mg/ml |
HEK293-derived CD5L retains native glycosylation patterns, unlike E. coli-produced versions, which lack glycosylation .
Immune Cell Studies: Used to investigate macrophage polarization and apoptosis resistance .
Metabolic Disease Models: Applied in obesity and atherosclerosis research to study lipid trafficking and inflammation .
Structural Biology: AlphaFold2 modeling reveals CD5L’s interaction with IgM and J-chain, aiding receptor-binding studies .
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 .