Analytical Data
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Gene name
ASS1
- Application
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Alternative Names
ASS1；ASS；Argininosuccinate synthase
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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
P00966
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Expression Region
1-412aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF IEDVSREFVEEFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLELFMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK
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Molecular Weight
49 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
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Protein Description
ASS1 (Argininosuccinate synthase 1) is an essential enzyme involved in the urea cycle, which plays a critical role in the metabolism of nitrogen in mammals. Deficiency in the ASS1 enzyme can lead to a rare genetic disorder known as argininosuccinic aciduria, characterized by the accumulation of ammonia and argininosuccinate in the body, leading to severe neurological symptoms and developmental issues. Research on recombinant ASS1 protein focuses on understanding its structure, function, and regulatory mechanisms to develop potential therapeutic strategies for patients affected by this condition. By employing techniques such as molecular cloning, expression in various systems (e.g., bacteria, yeast, or mammalian cells), and purification methods, scientists aim to produce large quantities of functional ASS1. Furthermore, detailed studies of its enzymatic activity, interaction with other proteins, and response to metabolic changes are crucial for elucidating the pathophysiology of ASS1-related diseases. The development of recombinant ASS1 has potential applications not only in treating argininosuccinic aciduria but also in exploring the broader implications of the urea cycle in various metabolic disorders. Overall, the study of recombinant ASS1 protein provides a vital insight into nitrogen metabolism and offers a pathway towards innovative treatments for metabolic dysfunctions linked to this critical enzyme.
