Analytical Data
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Gene name
Arginase-1/ARG1
- Application
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Alternative Names
ARG1; Arginase I; Liver Arginase
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P07824
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Expression Region
Met1~Lys323
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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
Arginase-1 (ARG1), an enzyme that is crucial for the urea cycle, catalyzes the conversion of L-arginine to L-ornithine and urea. This enzyme plays a pivotal role not only in nitrogen metabolism but also in the regulation of various physiological and pathological processes, including immune response, tissue repair, and even cancer progression. Elevated ARG1 levels have been associated with the promotion of tumor growth and evasion of immune surveillance, as it can modulate immune cell function by depleting L-arginine, an essential amino acid for T cell activation. Consequently, researchers have focused on producing recombinant ARG1 proteins to better understand its enzymatic activity, regulation, and potential therapeutic applications. Recombinant protein studies have enabled the investigation of ARG1's structure-function relationships, as well as its interaction with inhibitors and substrates. Additionally, recombinant ARG1 can serve as a valuable tool for developing targeted therapies aimed at normalizing arginine metabolism in cancer and other diseases characterized by ARG1 overactivity. As a result, the exploration of ARG1 as both a biomarker and a therapeutic target has garnered significant interest in the fields of immunology and oncology, highlighting the need for more in-depth studies on its biological functions and clinical implications.
