Analytical Data
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Gene name
ARG
- Application
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Alternative Names
ARG1; Arginase I; Liver Arginase
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Species
Human
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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
P05089
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Expression Region
Met1~Lys322
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Molecular Weight
37kDa
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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
ARG (Arginine-rich protein) recombinant proteins have drawn significant attention in recent years due to their diverse biological functions and potential applications in various fields, including therapeutics and biotechnology. These proteins, characterized by their high arginine content, play crucial roles in cellular processes such as gene regulation, cell signaling, and protein interactions. Research has shown that ARG proteins can influence the stability and activity of other proteins, as well as modulate the immune response. Their unique structural characteristics facilitate the interaction with nucleic acids, making them valuable tools in gene delivery systems and molecular biology studies. Advances in recombinant DNA technology have enabled the production of these proteins in large quantities, allowing for detailed studies of their structure-function relationships. Additionally, ARG proteins have shown promise in drug delivery and as novel therapeutic agents, particularly in targeting cancer cells and combating infectious diseases. As the understanding of ARG proteins continues to evolve, their potential applications in personalized medicine and targeted therapies are becoming increasingly evident, underscoring the importance of continued research in this field. This growing interest in ARG recombinant proteins not only enhances our understanding of fundamental biological mechanisms but also paves the way for innovative solutions to complex health challenges.
