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Conditions of optimal ASL Enzyme performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
Phone: 1-617-401-8149
Fax: 1-617-606-5019
Email: message@sydlabs.com
Or leave a message with a formal purchase
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Introduction
Argininosuccinate lyase (ASL) is a member of the lyase 1 family. ASL is an enzyme which catalyzes the reversible breakdown of Argininosuccinate (ASA) yielding the amino acids arginine and fumarate. ASL which is located in the liver cytosol is the 4th enzyme of the urea cycle and involved in the biosynthesis of arginine in all species and the production of urea in ureotelic species. While Argininosuccinate synthetase (ASS) catalyzes the formation of argininosuccinate from citrulline and aspartate, ASL breaks down the newly formed argininosuccinate into L-arginine and fumarate. L-arginine continues within the urea cycle to form urea and orinthine, whereas fumarate can enter the citric acid cycle. ASL gene Mutations result in the autosomal recessive disorder argininosuccinic aciduria, or argininosuccinic acid lyase deficiency.
BP002561-ENZ-185: Recombinant Human Argininosuccinate Lyase (ASL) Enzyme
Source: E. coli-derived.
A single, non-glycosylated polypeptide chain containing 484 amino acids (1-464) and having a molecular mass of 53.8 kDa. ASL is fused to a 20 amino acid His-tag at N-terminus.
Purity: > 95.0% as determined by SDS-PAGE.
Formulation: The ASL solution (0.5 mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0), 2 mM DTT, 10% glycerol and 100 mM NaCl.
Shipping: The product is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
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