protein

SPEB Protein, E.coli (His-SUMO)

HY-P72072

5 μg;10 μg;50 μg

182;309;865 USD

SPEB Protein, E.coli (His-SUMO)

proteins

E. coli

5 μg;10 μg;50 μg

182;309;865 USD

The SPEB protein plays a central role in cellular processes as it catalyzes the formation of putrescine from agmatine. This enzyme activity is essential for the biosynthesis of putrescine, a polyamine with important functions in cell growth, proliferation, and various physiological processes. SPEB Protein, E.coli (His-SUMO) is the recombinant E. coli-derived SPEB protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag. The total length of SPEB Protein, E.coli (His-SUMO) is 306 a.a., with molecular weight of ~49.5 kDa.

E.coli

SPEB, or agmatine ureohydrolase, is an enzyme that catalyzes the formation of putrescine from agmatine. This enzymatic reaction is a crucial step in the biosynthetic pathway of polyamines. Putrescine is a diamine that serves as a precursor for the synthesis of higher polyamines, such as spermidine and spermine, which are essential for various cellular processes, including cell growth, differentiation, and nucleic acid stabilization. By converting agmatine into putrescine, SPEB plays a central role in regulating polyamine levels, influencing cellular functions critical for growth and development. It has to succinctly outline SPEB's specific catalytic activity in the biosynthesis of putrescine, emphasizing its importance in the polyamine metabolic pathway.

speB; EC55989_3229; Agmatinase; EC 3.5.3.11; Agmatine ureohydrolase; AUH

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

Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US;may vary elsewhere.