Anti-Argininosuccinate Lyase/ASL Antibody Picoband® Fluoro488 Conjugated

ASL (argininosuccinatelyase, also known as argininosuccinase) is an enzyme that catalyzes the reversible breakdown of argininosuccinate (ASA) producing the amino acid arginine and dicarboxylic acid fumarate. Located in liver cytosol, ASL is the fourth enzyme of the urea cycle and involved in the biosynthesis of arginine in all species and the production of urea in ureotelic species. Mutations in ASL, resulting low activity of the enzyme, increase levels of urea in the body and result in various side effects. The ASL gene is located on chromosome 7 between the centromere (junction of the long and short arm) and the long (q) arm at position 11.2, from base pair 64,984,963 to base pair 65,002,090.

A synthetic peptide corresponding to a sequence at the N-terminus of human Argininosuccinate Lyase/ASL, which shares 97.4% and 92.1% amino acid (aa) sequence identity with mouse and rat Argininosuccinate Lyase/ASL, respectively.

Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.

1. Sampaleanu LM, Vallée F, Thompson GD, Howell PL (December 2001) . Three-dimensional structure of the argininosuccinatelyase frequently complementing allele Q286R. Biochemistry. 40 (51) : 15570–80. 2. Yu B, Howell PL (October 2000) . Intragenic complementation and the structure and function of argininosuccinatelyase. Cell. Mol. Life Sci. 57 (11) : 1637–51.