Analytical Data
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Gene name
argF
- Application
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Alternative Names
OTCase-2
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His
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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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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
Related Products
Protein Description
The argF gene encodes an enzyme involved in the biosynthetic pathway of arginine, an essential amino acid that plays a crucial role in various physiological processes, including protein synthesis, cell division, and the production of nitric oxide. Understanding the function of argF and the enzymes it encodes has significant implications for fields such as microbiology, medicine, and biotechnology. In particular, recombinant protein studies using argF can provide insights into metabolic engineering and the development of novel therapeutic agents. Researchers have sought to produce recombinant argF proteins to elucidate their structure and activity, aiming to explore their potential applications in metabolic pathways. Techniques such as gene cloning, expression in suitable host systems, and purification methods have been employed to generate functional argF proteins. Characterization of these recombinant proteins allows for a deeper understanding of their enzymatic properties, substrate specificity, and regulatory mechanisms. Furthermore, studying argF may contribute to the development of strategies for the bioengineering of microorganisms, enhancing their ability to synthesize arginine and other metabolites of economic interest. The overarching goal of these investigations is to leverage the knowledge gained from argF studies to influence agricultural practices, improve health supplements, and foster innovation in biotechnological applications.
