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Human ARG1 / Arginase 1 Protein (His Tag)

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Human ARG1 Protein Product Information
Protein Construction:A DNA sequence encoding the human ARG1 isoform 1 (P05089-1) (Met 1-Lys 322) was fused with a polyhistidine tag at the C-terminus.
Expressed Host:Human Cells
Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Human ARG1 Protein QC Testing
Purity:> 90 % as determined by SDS-PAGE
Bio-Activity:Measured by the production of urea during the hydrolysis of arginine.
The specific activity is >35,000 pmoles/min/μg.
Endotoxin:< 1.0 EU per μg of the protein as determined by the LAL method
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Met 1
Molecule Mass:The secreted recombinant human ARG1 consists of 333 amino acids and has a calculated molecular mass of 36.2 kDa. The apparent molecular mass of the protein is approximately 40 kDa in SDS-PAGE under reducing conditions.
Formulation:Lyophilized from sterile 20mM Tris, 150mM NaCl, 20% Glycerol, 1mM DTT, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Human ARG1 Protein Usage Guide
Storage: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.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Other ARG1 Recombinant Protein Products
ARG1/Arginase 1 Background

Arginase is the focal enzyme of the urea cycle hydrolysing L-arginine to urea and L-ornithine. Emerging studies have identified arginase in the vasculature and have implicated this enzyme in the regulation of nitric oxide (NO) synthesis and the development of vascular disease. Arginase also redirects the metabolism of L-arginine to L-ornithine and the formation of polyamines and L-proline, which are essential for smooth muscle cell growth and collagen synthesis. Arginase is encoded by two recently discovered genes (Arginase I and Arginase II). In most mammals, Arginase 1 (ARG1) also known as Arginase, liver, which functions in the urea cycle, and is located primarily in the cytoplasm of the liver. The second isozyme, Arginase II, has been implicated in the regulation of the arginine/ornithine concentrations in the cell. It is located in mitochondria of several tissues in the body, with most abundance in the kidney and prostate. It may be found at lower levels in macrophages, lactating mammary glands, and brain.

Human ARG1/Arginase 1 References
  • Durante W, et al. (2007) Arginase: a critical regulator of nitric oxide synthesis and vascular function. Clin Exp Pharmacol Physiol. 34(9): 906-11.
  • Waddington SN. (2002) Arginase in glomerulonephritis. Kidney Int. 61(3): 876-81.
  • Morris SM. (2002). Regulation of enzymes of the urea cycle and arginine metabolism. Annual review of nutrition. 22 (1): 87-105.
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    Catalog: 11558-H08H-10
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