protein

LpxC Protein, E.coli (His)

HY-P71488

5 μg;10 μg;50 μg

110;190;530 USD

LpxC Protein, E.coli (His)

proteins

E. coli

5 μg;10 μg;50 μg

110;190;530 USD

LpxC protein serves as a key enzyme in lipid A biosynthesis by catalyzing the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine, marking a key and crucial step in this important pathway. Through this enzymatic process, LpxC promotes the conversion of its substrate into UDP-3-O-myristoylglucosamine and acetate, making a significant contribution to lipid A biosynthesis. LpxC Protein, E.coli (His) is the recombinant E. coli-derived LpxC protein, expressed by E. coli , with N-His labeled tag.

E.coli

LpxC is an enzyme that plays a crucial role in lipid A biosynthesis by catalyzing the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine. This reaction results in the formation of UDP-3-O-myristoylglucosamine and acetate, representing the committed step in the biosynthesis of lipid A, a key component of bacterial lipopolysaccharides. Lipid A is an essential structural element in the outer membrane of Gram-negative bacteria, contributing to membrane integrity and playing a role in host-pathogen interactions. LpxC's catalytic activity is pivotal for the production of lipid A, and the enzyme serves as a potential target for the development of antibacterial agents aimed at disrupting the synthesis of crucial bacterial cell wall components.

lpxC; asmB; envA; b0096; JW0094; UDP-3-O-acyl-N-acetylglucosamine deacetylase; UDP-3-O-acyl-GlcNAc deacetylase; EC 3.5.1.108; Protein EnvA; UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase

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

Lyophilized after extensive dialysis against solution in 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.