CLEC4E Protein, Human (HEK293, His)

CLEC4E Protein is a calcium-dependent lectin that serves as a pattern recognition receptor (PRR) in the innate immune system. It is responsible for detecting and binding to damage-associated molecular patterns (DAMPs) of abnormal self and pathogen-associated molecular patterns (PAMPs) found in bacteria and fungi. Notably, it can recognize mycobacterial trehalose 6,6'-dimycolate (TDM), a glycolipid with potent immunomodulatory functions. In myeloid cells, CLEC4E interacts with the signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex. Binding of TDM to this receptor complex triggers phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, leading to activation of SYK, CARD9, and NF-kappa-B. This ultimately drives the maturation of antigen-presenting cells and shapes antigen-specific priming of T-cells towards effector T-helper 1 and T-helper 17 cell subtypes. CLEC4E also recognizes alpha-mannose residues on pathogenic fungi, such as Malassezia, and mediates macrophage activation. Additionally, CLEC4E enables immune sensing of damaged self by recognizing DAMPs released during nonhomeostatic cell death, thereby promoting inflammatory cell infiltration into the damaged tissue. CLEC4E can exist as a monomer or homodimer and interacts directly with FCER1G to form a functional complex. Alternatively, it acts as a bridge for interaction between CLEC4D and FCER1G. Furthermore, CLEC4E can directly interact with SAP130 nuclear protein, which is released from necrotic cells.