C-Type Lectin Domain Family 10, Member A Human Recombinant
CLEC10A Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 241 amino acids (61-292a.a.) and having a molecular mass of 27.3kDa. (Molecular size on SDS-PAGE under reducing conditions 28-40kDa).
CLEC10A is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
C-type Lectin Domain Family 4, Member M Human Recombinant
CLEC4M Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 570 amino acids (72-399 a.a) and having a molecular mass of 64.8kDa.
CLEC4M is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Sterile filtered colorless solution.
C-Type Lectin Domain Family 5, Member A Human Recombinant
C-Type Lectin Domain Family 5, Member A Human Recombinant, Sf9
CLEC5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (28-188 a.a.) and fused to a 9 aa His Tag at C-terminus containing a total of 170 amino acids and having a molecular mass of 19.5kDa.
CLEC5A shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
C-Type Lectin Domain Family 7, Member A Human Recombinant
CLEC7A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 183 amino acids (71-244 a.a) and having a molecular mass of 21kDa. CLEC7A is fused to a 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
C-type Lectin Domain Family 1, Member B Human Recombinant
C-type Lectin Domain Family 1, Member B, Human Recombinant, Sf9
C-type Lectin Domain Family 2, Member B Human Recombinant
C-type Lectin Domain Family 2, Member B Human Recombinant, Sf9
CLEC2B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 366 amino acids (26-149a.a.) and having a molecular mass of 41.7kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
CLEC2B is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques
Sf9, Baculovirus cells.
C-type Lectin Domain Family 2, Member D Human Recombinant
CLEC2D Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (60-191 a.a.) and having a molecular mass of 17.7 kDa.
CLEC2D is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Escherichia Coli.
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 .