HSD17B10 Protein, Human (sf9, GST)

HSD17B10 Protein, Human (sf9, GST) is the recombinant human-derived HSD17B10, expressed by Sf9 insect cells , with GST labeled tag. ,

ERAB is a mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid, and steroid metabolism. It acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, catalyzing the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA, with a preference for straight medium- and short-chain acyl-CoA substrates, most efficiently for (3S)-hydroxybutanoyl-CoA. In branched-chain amino acid catabolism, it functions as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase, oxidizing 3-hydroxy-2-methylbutanoyl-CoA in the isoleucine degradation pathway. It also exhibits hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids, oxidizing 3alpha-, 17beta-, 20beta-, and 21-hydroxysteroids as well as 7alpha- and 7beta-hydroxy bile acids. Additionally, ERAB has phospholipase C-like activity toward cardiolipin and its oxidized species, potentially degrading these during oxidative stress to protect cells from apoptosis. Interaction with intracellular amyloid-beta may contribute to neuronal dysfunction in Alzheimer's disease. ERAB is essential for mitochondrial structural and functional integrity. by similar: ERAB also moonlights as a component of mitochondrial ribonuclease P, which cleaves tRNA at the 5'-end. It forms the MRPP1-MRPP2 subcomplex with TRMT10C/MRPP1, catalyzing the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 in tRNAs and serving as a tRNA maturation platform to enhance 3'-processing by ELAC2.

Human

Sf9 insect cells

GST

Q99714-1 (M1-P261)

3028

Full Length of Isoform-1

MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVIRLDGAIRMQP

≥ 95%, as determined by reducing SDS-PAGE.