Analytical Data
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Gene name
ASL
- Application
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Alternative Names
ASL；Argininosuccinate lyase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
2-464aa
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AA Sequence
ASESGKLWG GRFVGAVDPI MEKFNASIAY DRHLWEVDVQ GSKAYSRGLE KAGLLTKAEM DQILHGLDKV AEEWAQGTFK LNSNDEDIHT ANERRLKELI GATAGKLHTG RSRNDQVVTD LRLWMRQTCS TLSGLLWELI RTMVDRAEAE RDVLFPGYTH LQRAQPIRWS HWILSHAVAL TRDSERLLEV RKRINVLPLG SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA EFLFWASLCM THLSRMAEDL ILYCTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMS AVLQVATGVI STLQIHQENM GQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET KGVALNQLSL QELQTISPLF SGDVICVWDY GHSVEQYGAL GGTARSSVDW QIRQVRALLQ AQQA
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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
ASL (Argininosuccinate lyase) is an enzyme that plays a crucial role in the urea cycle, which is vital for removing excess nitrogen from the body by converting argininosuccinate into arginine and fumarate. Deficiencies in this enzyme can lead to argininosuccinic aciduria, a rare genetic disorder characterized by the accumulation of toxic metabolites that may cause severe neurological damage and developmental delays. Research on ASL recombinant proteins has gained attention due to their potential therapeutic applications, including enzyme replacement therapy for patients with ASL deficiency. Advances in recombinant DNA technology have enabled the production of large quantities of functional ASL proteins, facilitating detailed studies of their structure and function. By understanding the enzyme's kinetics, stability, and interaction with substrates, researchers aim to develop targeted therapies that can mitigate the effects of the deficiency. Additionally, establishing a robust production system for ASL can pave the way for gene therapy approaches, where the enzyme is delivered directly to patients to restore normal metabolic function. Overall, the study of ASL recombinant proteins not only enhances our understanding of the enzyme's biological role but also holds promising avenues for clinical interventions in metabolic disorders related to the urea cycle.
