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  • 产品名称：Arginase,Liver(ARG1)(AA1-322)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
Arginase,Liver(ARG1)(AA1-322)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 35.6 kDa. The protein migrates as 36 kDa under reducing (R) condition (SDS-PAGE).
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured by the production of urea during the hydrolysis of arginine. The specific activity is >35,000 pmol/min/μg.
Background Arginase-1 (ARG1) is also known as Liver-type arginase, Type I arginase, which belongs to the arginase family. Arginase-1 / ARG1 is a manganese-containing enzyme. The reaction catalyzed by this enzyme is: arginine + H2O → ornithine + urea. It is the final enzyme of the urea cycle. Defects in Arginase-1 / ARG1 are the cause of argininemia (ARGIN).
Molecular Weight 35.6 kDa
NCBI Accession NP_000036
UniProt P05089
Pathways Cellular Response to Molecule of Bacterial Origin
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 150 mM NaCl, pH 7.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Arginase, Liver (ARG1) (AA 1-322) (Active) protein (His tag) (ABIN2180550) Human Arginase 1, His Tag on SDS-PAGE under reducing (R) condition. The gel was stain...
Background publications Shishova, Di Costanzo, Cane, Christianson: "X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate." in: Biochemistry, Vol. 46, Issue 7, pp. 1941-51, 2007 (PubMed).

Di Costanzo, Pique, Christianson: "Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster." in: Journal of the American Chemical Society, Vol. 129, Issue 20, pp. 6388-9, 2007 (PubMed).

Di Costanzo, Sabio, Mora, Rodriguez, Ochoa, Centeno, Christianson: "Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, Issue 37, pp. 13058-63, 2005 (PubMed).

Ikemoto, Tabata, Miyake, Kono, Mori, Totani, Murachi: "Expression of human liver arginase in Escherichia coli. Purification and properties of the product." in: The Biochemical journal, Vol. 270, Issue 3, pp. 697-703, 1990 (PubMed).