Name :
Recombinant Human Arginase 1/ARG1 Protein (His Tag)
Biological Activity :
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.
Biological Activity :
Measured by the production of urea during the hydrolysis of arginine.The specific activity is >35,000 pmoles/min/μg.
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
P05089-1
NCBI Gene ID :
Synonyms :
Synonyms :
arginase 1
Amino Acid Sequence :
Molecular Weight :
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.
Purity :
> 90 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
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.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
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.
Buffer Solution :
Supplied as sterile 20mM Tris, 150mM NaCl, 20% Glycerol, 1mM DTT, pH 7.4Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Synonyms :
ARG1 Protein, Human Arginase 1/ARG1 背景信息 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.
References & Citations :
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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