ALDH4A1 Protein, Human (sf9, His-GST)

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, His-GST) is the recombinant human-derived ALDH4A1 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of ALDH4A1 Protein, Human (sf9, His-GST) is 539 a.a., with molecular weight of ~75 KDa.

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.

Human

Sf9 insect cells

N-His;N-GST

P30038 (K25-Q563)

8659  [NCBI]

Approximately 75 kDa.

Greater than 80% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.