C-Type Lectin Domain Family 10, Member A Human Recombinant
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, a glycosylated polypeptide chain, is produced in Sf9 Baculovirus cells. This recombinant protein consists of 366 amino acids (26-149a.a.) with a molecular mass of 41.7kDa. However, the molecular size on SDS-PAGE may appear between 40-57kDa. The protein is expressed with a 242 amino acid hIgG-His tag at the C-terminus and purified using proprietary chromatographic techniques.
Sf9, Baculovirus cells.
C-type Lectin Domain Family 2, Member D Human Recombinant
Escherichia Coli.
C-Type Lectin Domain Family 7, Member A Human Recombinant
Sf9, Baculovirus cells.
C-type Lectin Domain Family 4, Member E Human Recombinant
C-type Lectin Domain Family 4, Member M Human Recombinant
This product consists of the extracellular domain of human CLEC4M, spanning amino acids 72 to 399, fused to a C-terminal 239 amino acid hIgG-His-Tag. This recombinant protein is expressed in Sf9 insect cells using a baculovirus expression system. The result is a glycosylated polypeptide with a molecular weight of 64.8 kDa. Following expression, the protein undergoes purification using proprietary chromatographic methods to ensure high purity.
Sf9, Baculovirus cells.
The purified CLEC4M protein solution appears colorless and is sterile-filtered.
C-Type Lectin Domain Family 5, Member A Human Recombinant
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 .