protein

ALDH4A1 Protein, Human (sf9)

HY-P76138

5 μg;10 μg;50 μg

95;160;440 USD

ALDH4A1 Protein, Human (sf9)

proteins

Sf9 insect cells

5 μg;10 μg;50 μg

95;160;440 USD

The ALDH4A1 protein is a key enzyme that irreversibly converts delta-1-pyrroline-5-carboxylate (P5C) to glutamate, a key step linking the urea and tricarboxylic acid cycles. ALDH4A1 prefers glutamate γ-semialdehyde but also accepts substrates such as succinate, glutaric acid, and adipic acid semialdehyde. ALDH4A1 Protein, Human (sf9) is the recombinant human-derived ALDH4A1 protein, expressed by Sf9 insect cells , with tag free. The total length of ALDH4A1 Protein, Human (sf9) is 539 a.a., with molecular weight of ~54 KDa.

Human

ALDH4A1, a pivotal enzyme, catalyzes the irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived from either proline or ornithine, into glutamate. This enzymatic transformation serves as a crucial step in the intricate pathway linking the urea and tricarboxylic acid cycles. The preferred substrate for ALDH4A1 is glutamic gamma-semialdehyde, while it also accepts other substrates such as succinic, glutaric, and adipic semialdehydes. The enzymatic activity of ALDH4A1 plays a central role in maintaining the metabolic balance between proline, ornithine, and glutamate, contributing to the efficient utilization of these amino acids within the interconnected cellular pathways.

Delta-1-pyrroline-5-carboxylate dehydrogenase; P5C dehydrogenase; ALDH4; P5CDH

Greater than 95% as determined by reducing SDS-PAGE

Supplied as a 0.22 μm filtered solution of 20 mM Tris, 500 mM NaCl, 10% glycerol, pH 8.5.

Shipping with dry ice