DLST Protein, Human (sf9, His)

The DLST protein is part of the 2-oxoglutarate dehydrogenase complex, which converts 2-oxoglutarate into succinyl-CoA and CO(2). It is active in the mitochondrion and plays a role in histone succinylation in the nucleus by supplying succinyl-CoA to the histone succinyltransferase KAT2A. DLST Protein, Human (sf9, His) is the recombinant human-derived DLST protein, expressed by Sf9 insect cells , with N-His labeled tag. The total length of DLST Protein, Human (sf9, His) is 386 a.a., with molecular weight of ~43.9 kDa.

DLST protein functions as the dihydrolipoamide succinyltransferase (E2) component within the 2-oxoglutarate dehydrogenase complex, a key player in cellular metabolism. This complex catalyzes the conversion of 2-oxoglutarate to succinyl-CoA and CO(2), predominantly operating in the mitochondrion. Notably, a fraction of the 2-oxoglutarate dehydrogenase complex localizes in the nucleus, where DLST is crucial for lysine succinylation of histones. DLST associates with KAT2A on chromatin, providing succinyl-CoA to histone succinyltransferase KAT2A. This dual localization underscores DLST's pivotal role in coordinating metabolic processes within the mitochondria and contributing to epigenetic modifications in the nucleus, highlighting its multifaceted functionality in cellular homeostasis.

Human

Sf9 insect cells

N-His

P36957 (D68-L453)

1743  [NCBI]

Approximately 43.9 kDa

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

<1 EU/μg, determined by LAL method.