protein

HMBS/Porphobilinogen deaminase Protein, Human (HEK293, His)

HY-P70269

10 μg;50 μg

160;450 USD

HMBS/Porphobilinogen deaminase Protein, Human (HEK293, His)

proteins

HEK293

10 μg;50 μg

160;450 USD

HMBS (porphobilinogen deaminase) is key to heme biosynthesis, catalyzing the sequential polymerization of four porphobilinogen molecules to form hydroxymethylbiphenyl. The process begins with dipyrromethane cofactor assembly derived from porphobilinogen or preuroporphyrinogen and promoted by apoenzymes. HMBS/Porphobilinogen deaminase Protein, Human (HEK293, His) is the recombinant human-derived HMBS/Porphobilinogen deaminase protein, expressed by HEK293 , with C-6*His labeled tag.

Human

HMBS, also known as Porphobilinogen deaminase, plays a crucial role in the heme biosynthetic pathway by catalyzing the sequential polymerization of four molecules of porphobilinogen, leading to the formation of hydroxymethylbilane, also referred to as preuroporphyrinogen. The catalytic process initiates with the assembly of the dipyrromethane cofactor, derived either from two molecules of porphobilinogen or from preuroporphyrinogen, by the apoenzyme. This covalently linked cofactor serves as a primer, facilitating the assembly of the tetrapyrrole product. In the final step of catalysis, the product preuroporphyrinogen is released, leaving the intact cofactor bound to the holodeaminase. This enzymatic activity is pivotal for the synthesis of heme, a crucial component with diverse biological functions.

rHuPorphobilinogen deaminase/HMBS, His; Porphobilinogen Deaminase; PBG-D; Hydroxymethylbilane Synthase; HMBS; Pre-Uroporphyrinogen Synthase; HMBS; PBGD; UPS

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

Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, 5% Trehalose, 5% mannitol, 50% Glycerol, 0.1% Tween80, pH 7.4.

Room temperature in continental US; may vary elsewhere.