Argininosuccinate lyase Protein, Human (sf9, His-GST)

Argininosuccinate lyase catalyzes the reversible cleavage of L-argininosuccinate, a key step in the urea cycle for hepatic nitrogen detoxification and de novo synthesis of L-arginine. Argininosuccinate lyase Protein, Human (sf9, His-GST) is the recombinant human-derived Argininosuccinate lyase protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of Argininosuccinate lyase Protein, Human (sf9, His-GST) is 464 a.a., with molecular weight of ~68 kDa.

The Argininosuccinate lyase protein assumes a critical role in nitrogen detoxification and L-arginine synthesis by catalyzing the reversible cleavage of L-argininosuccinate into fumarate and L-arginine, a pivotal intermediate reaction in the urea cycle. This process primarily occurs in the liver, contributing to hepatic nitrogen detoxification by converting nitrogenous waste into excretable urea. Moreover, Argininosuccinate lyase is essential for de novo L-arginine synthesis in nonhepatic tissues. Beyond its role in the urea cycle, this protein serves as a crucial regulator of intracellular and extracellular L-arginine pools. As part of the citrulline-nitric oxide cycle, Argininosuccinate lyase forms tissue-specific multiprotein complexes with argininosuccinate synthase ASS1, transport protein SLC7A1, and nitric oxide synthase NOS1, NOS2, or NOS3. This complex allows for cell-autonomous L-arginine synthesis and channels extracellular L-arginine into the nitric oxide synthesis pathway, underscoring its multifaceted role in cellular homeostasis and nitrogen metabolism.

Human

Sf9 insect cells

N-His;N-GST

P04424 (M1-A464)

435  [NCBI]

Approximately 68 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.