Lysosome-associated membrane protein 2 (LAMP-2), also known as CD107b, is an abundant lysosomal integral membrane glycoprotein.{51235,51232} It is composed of a signal peptide, two LAMP-like domains that are separated by a proline-rich hinge region, a transmembrane domain, and a C-terminal tail that contains a YXXF tyrosine-based motif, which is required for targeting of LAMP-2 to the lysosome. Alternative splicing produces three isoforms, LAMP-2A, LAMP-2B, and LAMP-2C, which are involved in chaperone-mediated autophagy, macroautophagy, or RNautophagy/DNautophagy, respectively.{15803,68308} LAMP-2A and LAMP2C are ubiquitously expressed, but LAMP-2B is localized to skeletal and cardiac muscle and brain tissues.{68308} In addition to its role in autophagy, LAMP-2 is also involved in human peripheral blood mononuclear cell (PBMC) adhesion to vascular endothelium and ferroptosis.{15784,43753} Knockout of Lamp2 increases mortality and reduces heart contractility.{15804} Mutations in LAMP2 cause Danon disease, an X-linked disorder characterized by skeletal myopathy and hypertrophic cardiomyopathy and cognitive impairment.{68308} Cayman’s LAMP-2/CD107b Monoclonal Antibody (Clone GL2A7) can be used for immunocytochemistry (ICC), immunofluorescence (IF), immunoprecipitation (IP), and Western blot (WB) applications. The antibody recognizes LAMP-2 at approximately 100-110 kDa from human, mouse, and rabbit samples.