CD107b, also known as lysosome-associated membrane protein-1 (LAMP-1), is a transmembrane glycoprotein predominantly localized in lysosomes and late endosomes. It belongs to the LAMP family, which plays critical roles in maintaining lysosomal integrity, regulating autophagy, and facilitating vesicular trafficking. CD107b is a heavily glycosylated protein with a molecular weight of approximately 110-120 kDa, characterized by a luminal domain with conserved N-linked glycosylation sites and a short cytoplasmic tail. Its expression on the plasma membrane increases during cellular activation or stress, particularly in immune cells like cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells, where it serves as a marker of degranulation.
Antibodies targeting CD107b are widely used in flow cytometry and immunofluorescence to study lysosomal exocytosis, immune cell functionality, and cellular responses to pathogens or tumors. In research, surface CD107b detection helps quantify the release of lytic granules during immune responses, correlating with cytotoxic activity. Additionally, CD107b antibodies aid in investigating lysosomal disorders, neurodegenerative diseases, and cancer biology, as altered LAMP-1 expression is linked to tumor progression, metastasis, and immune evasion. Its role in cell adhesion and phagosome-lysosome fusion further underscores its relevance in infectious disease studies. CD107b antibodies thus serve as essential tools for exploring lysosomal dynamics, immune mechanisms, and disease pathogenesis.