Anti-Human CD302 Antibody Pair

Product Description: CD302 molecule (CD302), also known as CLEC13A or DCL1, is a type I transmembrane C-type lectin receptor primarily involved in cell adhesion, migration, endocytosis, and phagocytosis. Structurally, it is a 232-amino-acid protein with a 146-amino-acid extracellular domain, a 21-amino-acid transmembrane segment, and a 43-amino-acid cytoplasmic region. The extracellular domain is predicted to contain eight beta strands and two alpha helices, and CD302 is highly conserved across species, sharing 82% sequence identity with its mouse and rat counterparts. Unlike classical C-type lectin receptors, CD302 lacks the amino acid residues necessary for calcium-dependent sugar binding, suggesting a unique ligand recognition mechanism. CD302 is most abundantly expressed in the liver, followed by the lungs, spleen, and myeloid cells such as monocytes, granulocytes, and dendritic cells. Disease relevance includes its identification as an intergenic splice variant forming a fusion protein with DEC-205/CD205 in Hodgkin's lymphoma cell lines, indicating a potential role in hematological malignancies. Protein Function: Potential multifunctional C-type lectin receptor that may play roles in endocytosis and phagocytosis as well as in cell adhesion and migration [The Uniprot Consortium]