SPEB Protein, Streptococcus pyogenes (His-SUMO)

SPEB Protein, Streptococcus pyogenes (His-SUMO) is the recombinant SPEB protein, expressed by E. coli, with N-6*His & N-SUMO tag.

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.

Others

E. coli

N-6*His;N-SUMO

P0C0J0 (Q146-P398)

69901512

Full Length of Mature Protein

QPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP

Approximately 40-45 kDa, based on SDS-PAGE under reducing conditions.

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

<1 EU/μg, determined by LAL method.