speA Protein, Shewanella putrefaciens (FLAG, His)

The speA protein plays a crucial role in catalyzing the transformation from arginine to agmatine. This enzymatic conversion highlights speA's significance in sustaining cellular metabolism and essential biological processes. By synthesizing agmatine, speA emerges as a key player in the intricate dance of molecular transformations that characterize fundamental cellular functions. speA Protein, Shewanella putrefaciens (FLAG, His) is the recombinant speA protein, expressed by E. coli , with N-6*His, N-Flag labeled tag. The total length of speA Protein, Shewanella putrefaciens (FLAG, His) is 637 a.a., .

The speA protein serves as a catalytic linchpin in the intricate biosynthetic journey from arginine to agmatine. With precision and enzymatic finesse, speA orchestrates the conversion, showcasing its pivotal role in this biochemical pathway. The transformation guided by speA underscores its indispensability in cellular metabolism, accentuating the protein's significance in sustaining the delicate equilibrium of essential biological processes within the cell. In catalyzing the synthesis of agmatine, speA emerges as a key player in the intricate dance of molecular transformations that characterize fundamental cellular functions.

Others

E. coli

N-6*His;N-Flag

A4Y5Y9 (M1-S637)

/

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

<1 EU/μg, determined by LAL method.