protein

SPEA Protein, E.coli (His)

HY-P71695

20 μg;50 μg;100 μg

235;450;720 USD

SPEA Protein, E.coli (His)

proteins

E. coli

20 μg;50 μg;100 μg

235;450;720 USD

SPEA is a key enzyme in cellular metabolism responsible for the biosynthesis of agmatine from arginine. This catalytic process involves the conversion of arginine to agmatine, thereby forming a complex network of biochemical pathways within the cell. SPEA Protein, E.coli (His) is the recombinant E. coli-derived SPEA protein, expressed by E. coli , with N-His labeled tag.

E.coli

SPEA, also known as agmatine ureohydrolase, is an enzyme that plays a central role in the biosynthesis of agmatine from arginine. Specifically, SPEA catalyzes the conversion of arginine into agmatine, a process crucial in the metabolism of nitrogen-containing compounds. This enzymatic activity is a key step in the arginine catabolic pathway, contributing to the generation of agmatine, a biogenic amine with diverse physiological functions. It has to underscore SPEA's role in the synthesis of agmatine, shedding light on its importance in cellular nitrogen metabolism and the broader implications of agmatine in various biological processes.

speA; b2938; JW2905; Biosynthetic arginine decarboxylase; ADC; EC 4.1.1.19

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized after extensive dialysis against solution in 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.