ALAS2 Protein, Human (His)

ALAS2 Protein catalyzes PLP-dependent condensation of succinyl-CoA and glycine, producing aminolevulinic acid (ALA) with CoA and CO2 by-products. It significantly contributes to heme formation in erythropoiesis, with catalytic activity reaching 75-85% of isoform 1. ALAS2 Protein, Human (His) is the recombinant human-derived ALAS2 protein, expressed by E. coli , with N-6*His labeled tag.

The ALAS2 protein serves a critical role in heme biosynthesis by catalyzing the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products, as corroborated by various studies. Notably, ALAS2 significantly contributes to heme production during erythropoiesis, essential for hemoglobin synthesis in red blood cells. This enzymatic activity is a pivotal step in the heme biosynthetic pathway, ensuring the generation of ALA, a precursor molecule crucial for subsequent steps in heme synthesis. The catalytic activity of ALAS2 is reported to be 75-85% of isoform 1 activity, emphasizing its importance in providing the necessary building blocks for hemoglobin production and erythropoiesis.

Human

E. coli

N-6*His

P22557 (Q50-A587)

212  [NCBI]

Full Length of Mature Protein

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