LMAN1 (Lectin, Mannose-Binding 1), also known as ERGIC-53 or F5F8D, is a transmembrane glycoprotein that functions as a cargo receptor in the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). It plays a critical role in the selective transport of glycoproteins, including coagulation factors V and VIII, by recognizing mannose-rich oligosaccharides. Mutations in the *LMAN1* gene are linked to combined deficiency of factors V and VIII (F5F8D), a rare autosomal recessive bleeding disorder characterized by reduced levels of these clotting factors.
LMAN1 antibodies are essential tools for studying intracellular protein trafficking, ER-Golgi dynamics, and disease mechanisms. In research, they are widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to visualize LMAN1 expression, localization, and interactions. These antibodies also aid in investigating secretory pathway defects, ER-associated degradation (ERAD), and viral infections (e.g., hepatitis C virus entry). Commercial LMAN1 antibodies are typically raised against specific epitopes, validated for species reactivity (human, mouse, rat), and available in monoclonal or polyclonal formats. Their applications extend to exploring cancer biology, as altered LMAN1 expression has been observed in certain tumors, suggesting potential roles in tumor progression or suppression.