epitope mapping near the N-terminus of LYAG of human origin
recommended for detection of precursor and mature Lysosomal alpha-glucosidase (LYAG) of mouse, rat and human origin by WB, IP, IF and ELISA; also reactive with additional species, including equine, bovine and porcine
LYAG Background Information Lysosomal a-glucosidase (LYAG), also designated acid a-glucosidase or acid maltase, is essential for the degradation of glycogen to glucose in lysosomes. LYAG is a protein belonging to the glycosyl hydrolase 31 family and resides soley in the lysosome. After translation, LYAG undergoes proteolytic processing to form two lengths of lysosomal a-glucosidase, and both N-terminal and C-terminal processing occur. Conduritol B epoxide (CBE) is a competitive inhibitor of LYAG. Defects in GAA, the gene encoding for LYAG, may cause Pompe disease, an autosomal recessive disorder characterized by cardiorespiratory insufficiency and glycogen accumulation in muscle tissues, causing muscular weakness. Mutations on the LYAG gene also cause glycogen storage disease II (GSD-II).
LYAG (P-15)
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LYAG (P-15): sc-49440. Western blot analysis of LYAG expression in non-transfected: sc-117752 (A) and human LYAG transfected: sc-115825 (B) 293T whole cell lysates.
