protein

Tryptophan Synthase Protein, E.coli (His)

HY-P71098

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

60;95;250;400;1200;1750 USD

Tryptophan Synthase Protein, E.coli (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

60;95;250;400;1200;1750 USD

The TrpA protein, especially its α subunit, plays a crucial role in catalyzing the aldol cleavage of indole glycerol phosphate to produce indole and glyceraldehyde 3-phosphate. This enzymatic activity highlights the importance of TrpA in the tryptophan biosynthetic pathway, providing an essential component of cellular processes. Tryptophan Synthase Protein, E.coli (His) is a recombinant protein dimer complex containing E. coli-derived Tryptophan Synthase protein, expressed by E. coli , with N-6*His labeled tag. Tryptophan Synthase Protein, E.coli (His), has molecular weight of 28 & 40-50 kDa, respectively.

E.coli

The TrpA protein, with its alpha subunit, takes on the crucial role of catalyzing the aldol cleavage of indoleglycerol phosphate, yielding indole and glyceraldehyde 3-phosphate. This enzymatic activity highlights the functional significance of TrpA in the tryptophan biosynthesis pathway, contributing to the generation of essential components for cellular processes. The alpha subunit's specific involvement in this cleavage reaction underscores its role as a key catalyst in the intricate biochemical machinery governing the synthesis of tryptophan in various biological contexts.

Tryptophan synthetase; Tryptophan synthase

Greater than 95% as determined by reducing SDS-PAGE.

Supplied as a 0.2 μm filtered solution of PBS, pH 7.4.

Shipping with dry ice.