Recombinant Human Argininosuccinate Lyase protein
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Recombinant Human Argininosuccinate Lyase protein is a Human Full Length protein, in the 1 to 464 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
Argininosuccinate lyase, ASAL, Arginosuccinase, ASL
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Argininosuccinate Lyase protein (AB113605)
15% SDS-PAGE showing ab113605 (3 μg) at approximately 53.8 kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
This enzyme is important for the breakdown of nitrogen molecules impacting amino acid metabolism. ASL does not operate as part of a larger complex but acts independently to facilitate the removal of nitrogenous waste. Through its action it produces arginine which serves as a vital precursor for the production of nitric oxide a critical signaling molecule in many physiological processes.
Pathways
ASL is integral to the urea cycle and amino acid metabolic pathways. The urea cycle is fundamental for ammonia detoxification while amino acid metabolic pathways involve protein turnover and energy production. Within the urea cycle ASL works alongside enzymes like argininosuccinate synthetase and arginase playing a pivotal role in converting excess nitrogen to urea which the body then excretes.
Specifications
Form
Liquid
Additional notes
ab113605 was purified using conventional chromatography techniques.
General info
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).
Sequence similarities
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Post-translational modifications
Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TSA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity.
Target data
Product promise
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