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Human ARG1 / Arginase 1 Protein (His & MYC Tag)

ARG1

Catalog Number P11558-H35H
Organism Species Human
Host Human Cells
Synonyms ARG1
Molecular Weight The recombinant human ARG1 consists of 338 amino acids and predicts a molecular mass of 36.7 kDa.
predicted N His
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE.
Protein Construction A DNA sequence encoding the human ARG1 (NP_000036.2) (Met1-Lys322) was expressed with a polyhistidine tag at the N-terminus and a myc tag at the C-terminus.
Bio-activity
Research Area Cancer |Signal transduction |Metabolism |Types of disease |Metabolism in Cancer
Formulation Lyophilized from sterile 20 mM Tris, 500 mM NaCl, 20 % glycerol, 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.
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.
Reference
  • 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.