ABHD10 Protein, Human (sf9, His)

ABHD10 Protein, an acyl-protein thioesterase, crucially hydrolyzes fatty acids from acylated residues in proteins. It regulates mitochondrial S-depalmitoylation of peroxiredoxin-5/PRDX5, modulating mitochondrial antioxidant capacity. ABHD10 also catalyzes mycophenolic acid acyl-glucuronide deglucuronidation, an active metabolite of the immunosuppressant drug mycophenolate. This dual functionality highlights ABHD10's diverse regulatory impact on lipid metabolism, mitochondrial function, and drug metabolism. ABHD10 Protein, Human (sf9, His) is the recombinant human-derived ABHD10 protein, expressed by Sf9 insect cells, with N-His labeled tag. The total length of ABHD10 Protein, Human (sf9, His) is 254 a.a., with molecular weight of ~32 kDa.

ABHD10 protein serves as an acyl-protein thioesterase, playing a crucial role in hydrolyzing fatty acids from acylated residues in proteins. Notably, it regulates the mitochondrial S-depalmitoylation of the nucleophilic active site residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, thereby modulating the antioxidant capacity of mitochondria. Beyond its involvement in redox homeostasis, ABHD10 catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, which is an active metabolite of the immunosuppressant drug mycophenolate. This dual functionality underscores the diverse regulatory impact of ABHD10 in cellular processes related to lipid metabolism, mitochondrial function, and drug metabolism.

Human

Sf9 insect cells

N-His

Q9NUJ1 (T53-N306)

55347  [NCBI]

Approximately 32 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.