NAD(H)-dependent dehydrogenase/reductase with a preference for cyclic substrates (By similarity) (PubMed:35150746). Catalyzes stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-proline, likely a detoxification mechanism for ketoprolines (PubMed:35150746). Mediates the formation of 2,5-dihydroxybenzoate (2,5-DHBA), a siderophore that chelates free cytoplasmic iron and associates with LCN2, thereby regulating iron transport and homeostasis while protecting cells against free radical-induced oxidative stress. The iron-siderophore complex is imported into mitochondria, providing an iron source for mitochondrial metabolic processes in particular heme synthesis (By similarity). May act as a 3-hydroxybutyrate dehydrogenase (PubMed:16380372).

Dehydrogenase/reductase SDR family member 6 (EC 1.1.1.-) ((R)-beta-hydroxybutyrate dehydrogenase) (3-hydroxybutyrate dehydrogenase type 2) (EC 1.1.1.30) (4-oxo-L-proline reductase) (EC 1.1.1.104) (Oxidoreductase UCPA) (Short chain dehydrogenase/reductase family 15C member 1)
BDH2 DHRS6 SDR15C1 UNQ6308/PRO20933 DHRS6; EFA6R; PRO20933; SDR15C1; UCPA-OR; UNQ6308

Q9BUT1

Human, Mouse, Rat

WB,IHC,IF,ICC,FC

WB 1:2000
IHC 1:50
IF 1:100
ICC 1:100-1:400
FC 1:100

26.5 kDa

Mouse

Full length human recombinant protein of human BDH2(NP_064524) produced in HEK293T cell.

Monoclonal

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Store at -20 °C. Stable for 12 months from date of receipt.