Recombinant Proteins
Product List
CLEC4E Human
C-type Lectin Domain Family 4, Member E Human Recombinant
Introduction
A C-type lectin (CLEC) is a type of carbohydrate-binding protein known as a lectin. The “C-type” designation is derived from their requirement for calcium for binding. Proteins that contain C-type lectin domains have a diverse range of functions, including cell-cell adhesion, immune response to pathogens, and apoptosis . C-type lectins are classified into several subgroups based on the order of the various protein domains in each protein. Drickamer et al. initially classified C-type lectins into seven subgroups, which was later expanded to include additional groups .
C-type lectins are expressed by numerous cells in the body, including hepatocytes, activated macrophages, dendritic cells, bone marrow, and epithelial cells in the intestines and lungs . They are often complex, multidomain proteins with a single protein module for sugar binding, termed the carbohydrate recognition domain (CRD). The expression of C-type lectins can be induced by factors such as interferon-γ, interleukin-4, and interleukin-6 during infection . Additionally, several types of cancer cells express elevated levels of lectin mRNA .
C-type lectins play crucial roles in the immune system, including pathogen recognition and the activation of immune responses. They are involved in cell-cell adhesion, immune response to pathogens, and apoptosis . In the innate immune system, interactions between lectins and carbohydrates are essential for activating the complement cascade and phagocytosis of potential pathogens . C-type lectins also play roles in cell development, cell signaling, and glycoprotein quality control .
C-type lectins interact with other molecules and cells through their carbohydrate recognition domains (CRDs). These domains bind to specific sugar ligands in a calcium-dependent manner . The binding of C-type lectins to their ligands can trigger downstream signaling cascades that lead to various cellular responses, including the activation of immune cells and the production of cytokines . Some C-type lectins can also act as pattern recognition receptors (PRRs), binding to ligands derived from fungi, bacteria, or viruses .
The expression and activity of C-type lectins are regulated by various mechanisms, including transcriptional regulation and post-translational modifications. Cytokines such as interleukin-10, interleukin-4, interleukin-13, and interferon-γ can differentially regulate the expression of C-type lectins . Post-translational modifications, such as oligomerization, can enhance the binding affinity of lectins for multivalent or clustered ligands on pathogenic organisms .
C-type lectins have various applications in biomedical research, diagnostic tools, and therapeutic strategies. They are involved in extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions . In diagnostic tools, C-type lectins can be used to detect specific carbohydrate structures on pathogens or cancer cells. Therapeutically, targeting C-type lectins may help modulate immune responses or deliver drugs to specific cells .
C-type lectins play roles throughout the life cycle, from development to aging and disease. They are involved in essential processes such as development, respiration, coagulation, angiogenesis, and inflammation . During infection and inflammatory responses, the expression of C-type lectins is upregulated to enhance the immune response . Additionally, C-type lectins contribute to immune homeostasis by recognizing and clearing apoptotic cells .
