hDDC Protein, Human (His, Strep)

hDDC protein plays a central role in neurotransmitter synthesis by catalyzing the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to produce dopamine and L-5-hydroxytryptophan to produce serotonin. hDDC Protein, Human (His, Strep) is the recombinant human-derived hDDC protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of hDDC Protein, Human (His, Strep) is 480 a.a., .

Human aromatic L-amino acid decarboxylase (hDDC) is an enzyme that plays a crucial role in neurotransmitter biosynthesis by catalyzing the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin. This enzymatic activity is a pivotal step in the synthesis of two key neurotransmitters, dopamine and serotonin, both of which are essential for the central nervous system's regulation of mood, behavior, and motor functions. The conversion of DOPA to dopamine by hDDC is particularly significant in the dopaminergic pathways, influencing motor control and emotional processes. The parallel conversion of L-5-hydroxytryptophan to serotonin underscores hDDC's role in serotoninergic pathways, crucial for mood and emotional regulation. It has to emphasize hDDC's specific contributions to neurotransmitter synthesis, highlighting its importance in maintaining the delicate balance of signaling molecules critical for neurological functions.

Human

E. coli

N-Strep;N-6*His

P20711 (M1-E480)

1644

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

<1 EU/μg, determined by LAL method.