Recombinant human Arginase 1/ARG1 protein

Specific activity is > 150, 000pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0pmole of arginine to urea per minute at pH 10.5 at 37C.

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 PK

Arginase is a manganese-containing enzyme which catalyzes the hydrolysis of arginine to ornithine and urea. It is the final enzyme of the urea cycle. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform functions in the urea cycle, and is located primarily in the cytoplasm of the liver. The type II isoform 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. Recombinant human ARG1, fused to His-tag at C-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

E.coli

Metabolism

35.8 kDa (330aa) confirmed by MALDI-TOF