LMAN1 (E2B6H) Rabbit mAb #13974

Mannose-binding lectin-1 (LMAN1, ERGIC-53) is a type I transmembrane lectin protein localized to the intermediate compartment between the endoplasmic reticulum and the Golgi body (ERGIC) (1). Interaction between the LMAN1 protein and MCFD2 forms an ERGIC cargo receptor that delivers proteins from the ER to the Golgi body (2,3). The LMAN1 protein contains an amino-terminal carbohydrate recognition domain (CRD) that binds target glycoproteins, a membrane proximal oligomerization domain required for cargo transport, a single transmembrane segment, and short cytoplasmic tail (3-5). LMAN1 functions as a cargo receptor responsible for transport of glycoproteins from the ER to ERGIC and Golgi body. Target proteins include coagulation factors V and VIII, cathepsin C, cathepsin Z, and α1-antitrypsin (6-8). Mutations in the corresponding LMAN1 gene can result in combined factors FV and FVIII deficiency, an autosomal recessive disorder characterized by spontaneous bleeding (9). Inactivating frameshift mutations in LMAN1 are found at high frequency in colorectal tumors with microsatellite instability and may contribute to tumorigenesis (10).