Analytical Data
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Gene name
Argininosuccinate lyase
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简介
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.
- Application
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Alternative Names
Argininosuccinate lyase; ASAL; Arginosuccinase; ASL
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Species
Human
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Source
Baculovirus
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Tag
N-His;N-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04424
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Expression Region
M1-A464
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Protein Length
Full Length
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Molecular Weight
68 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Argininosuccinate lyase (ASL) is an essential enzyme in the urea cycle, mainly responsible for catalyzing the conversion of argininosuccinate into arginine and fumarate. Deficiencies in ASL can lead to argininosuccinic aciduria, a rare yet serious metabolic disorder characterized by the accumulation of toxic metabolites and subsequent neurological damage. As a result, understanding the structure and function of ASL is critical for developing effective treatments for this condition. Research on recombinant ASL has gained momentum, allowing for the production of the enzyme in various expression systems, including bacteria and yeast. This approach not only facilitates the detailed study of the enzyme's biochemical properties but also enables the exploration of therapeutic interventions, such as gene therapy and enzyme replacement strategies. Additionally, recombinant ASL serves as a valuable tool for elucidating the mechanism of the urea cycle and identifying potential drug targets for related metabolic disorders. The advances in protein engineering techniques, such as site-directed mutagenesis and molecular dynamics simulations, further enhance the understanding of ASL's functionality, paving the way for innovations in disease management and treatment options for patients suffering from urea cycle disorders.
