ARG1 Human, Active
Arginase-1 liver, Arginase-1, liver, Arginase-1, liver A I, Al, ARG 1, ARG1, Arginase 1, Arginase liver, Arginase type I, Arginase1, Liver type arginase, Type I arginase.
Greater than 85.0% as determined by SDS-PAGE.
Description
ARG1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids ( 1-322aa ) and having a molecular mass of 35.8 kDa. ARG1 is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
Arginase-1, a key enzyme in the urea cycle, breaks down arginine into ornithine and urea. Mammals have two forms of arginase, each with unique characteristics like tissue distribution, cellular location, immune response, and physiological function. Found mainly in the liver, Arginase-1 resides in the cytoplasm. An inherited deficiency in this enzyme can lead to argininemia, an autosomal recessive disorder characterized by elevated ammonia levels in the blood.
Recombinant human ARG1, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 330 amino acids (1-322aa) with a molecular weight of 35.8 kDa. An 8 amino acid His tag is fused to the C-terminus of ARG1. The protein is purified using proprietary chromatographic methods.
The ARG1 protein solution (0.5mg/ml) is supplied in a buffer containing 20mM Tris-HCl (pH 8.0), 20% glycerol, 2mM DTT, and 100mM NaCl.
The purity is determined to be greater than 85.0% using SDS-PAGE analysis.
The enzyme exhibits a specific activity greater than 150,000 pmol/min/ug, defined as the quantity of enzyme required to hydrolyze 1.0 pmole of arginine to urea per minute at 37°C and a pH of 10.5.
Arginase-1 liver, Arginase-1, liver, Arginase-1, liver A I, Al, ARG 1, ARG1, Arginase 1, Arginase liver, Arginase type I, Arginase1, Liver type arginase, Type I arginase.
MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY GDLPFADIPN DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD HSLAIGSISG HARVHPDLGV IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYIL KTLGIKYFSM TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF TPATGTPVVG GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT LACFGLAREG NHKPIDYLNP PKLEHHHHHH.
Product Science Overview
Human Arginase-1 is a homotrimeric enzyme with a molecular weight of approximately 105 kDa . Each subunit contains a manganese (Mn²⁺) ion, which is vital for its catalytic activity. The Mn²⁺ ion forms a metal-bound hydroxyl ion that acts as a nucleophile, attacking the guanidinium carbon of the substrate arginine .
Arginase-1 is predominantly expressed in the liver, where it facilitates the final step of the urea cycle, converting L-arginine into L-ornithine and urea . This process is critical for the removal of excess nitrogen from the body. Additionally, ARG1 is involved in various metabolic pathways, including the synthesis of polyamines, proline, and glutamate .
Recombinant human Arginase-1 (rhARG1) is produced using recombinant DNA technology, typically expressed in E. coli . This recombinant form retains the enzymatic activity of the native protein and is used in various research and therapeutic applications. The specific activity of rhARG1 is determined by the production of urea during the hydrolysis of arginine, with values exceeding 6000 pmol/min/µg .
Recombinant human Arginase-1 has shown potential in treating several pathological conditions. By depleting circulating arginine, rhARG1 can mitigate various diseases, including cancer, inflammatory conditions, and microbial infections . The enzyme’s ability to modulate the immune response and reduce arginine levels makes it a promising candidate for therapeutic interventions.
