Anti-Human ASL Antibody Pair

Product Description: Argininosuccinate lyase (ASL) is a cytosolic enzyme that catalyzes the reversible cleavage of L-argininosuccinate into fumarate and L-arginine, a critical step in the urea cycle responsible for detoxifying ammonia in the liver. This reaction not only facilitates the removal of excess nitrogen by producing urea for excretion but also generates arginine, an amino acid essential for protein synthesis and nitric oxide production, which plays a key role in vascular regulation. The enzyme's mechanism involves an E1cb elimination reaction, with specific amino acids such as histidine, threonine, lysine, and serine contributing to proton abstraction and stabilization of intermediates during catalysis. Deficiency of ASL due to mutations in the ASL gene leads to argininosuccinic aciduria, a rare inherited disorder characterized by hyperammonemia, developmental delay, and liver dysfunction, underscoring the enzyme's importance in nitrogen metabolism and overall health. Protein Function: Catalyzes the reversible cleavage of L-argininosuccinate to fumarate and L-arginine, an intermediate step reaction in the urea cycle mostly providing for hepatic nitrogen detoxification into excretable urea as well as de novo L-arginine synthesis in nonhepatic tissues (PubMed:11747432, PubMed:11747433, PubMed:22081021, PubMed:2263616, PubMed:9045711). Essential regulator of intracellular and extracellular L-arginine pools. As part of citrulline-nitric oxide cycle, forms tissue-specific multiprotein complexes with argininosuccinate synthase ASS1, transport protein SLC7A1 and nitric oxide synthase NOS1, NOS2 or NOS3, allowing for cell-autonomous L-arginine synthesis while channeling extracellular L-arginine to nitric oxide synthesis pathway (PubMed:22081021) [The Uniprot Consortium]