Analytical Data
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Gene name
argF
- Application
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Alternative Names
argF;Ornithine carbamoyltransferase
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Species
E.coli
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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
P06960
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Expression Region
2-334aa
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AA Sequence
SDLYKKHFLKLLDFTPAQFTSLLTLAAQLKADKKNGKEVQKLTGKNIALIFEKDSTRTRCSFEVAAFDQGARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAQYAGVPVWNGLTNEFHPTQLLADLMTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLLAPKACWPEESLVAECSALAEKHGGKITLTEDVAAGVKGADFIYTDVWVSMGEAKEKWAERIALLRGYQVNAQMMALTDNPNVKFLHCLPAFHDDQTTLGKQMAKEFDLHGGMEVTDEVFESAASIVFDQAENRMHTIKAVMMATLGE
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Molecular Weight
40.7 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
The argF gene, a crucial component of the arginine biosynthesis pathway, encodes the enzyme N-acetylglutamate kinase (NAGK), which plays a significant role in the metabolic processes of various microorganisms. This gene is particularly interesting in the context of microbial ecology and biotechnology due to its function in nitrogen metabolism and regulation of amino acid synthesis. Research on argF recombination proteins focuses on understanding the structural and functional aspects of this enzyme, its regulation under different environmental conditions, and its evolutionary significance across different species. Studies have shown that the manipulation of argF can enhance arginine production, which is important not only for microbial growth but also for industrial applications, including the synthesis of fertilizers and pharmaceuticals. Additionally, characterizing argF and its associated pathways can provide insights into microbial responses to nutrient availability, which is vital for understanding ecological dynamics in natural environments. Consequently, the investigation of argF recombination proteins contributes to a broader understanding of metabolic engineering, offering potential avenues for the development of more efficient microbial strains tailored for specific biotechnological applications.











