Recombinant e.coli GladA-eiwit

GldA catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone) . This protein allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E. coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i. e. the conversion of dihydroxyacetone into glycerol. gldA possesses a broad substrate specificity, since it is also able to oxidize 1, 2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1, 2-propanediol, respectively. Recombinant E. coli gldA protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

Glycerol dehydrogenase, ECK3937, JW5556

E.coli

E.coli

His-Tag

SDS-PAGE

1 mg/mL (determined by Bradford assay)

> 95% by SDS-PAGE

41.1 kDa (390aa) confirmed by MALDI-TOF

GldA, Glycerol dehydrogenase, ECK3937, JW5556, ATGP2824-10 µg, ATGP2824-20 µg, ATGP2824-50 µg, ATGP2824-100 µg, ATGP2824-250 µg, ATGP2824-500 µg, ATGP2824-1 mg, ATGP2824-10, ATGP2824-20, ATGP2824-50, ATGP2824-100, ATGP2824-250, ATGP2824-500, ATGP2824-1

Subedi K.P., et al. (2008) FEMS Microbiol. Lett. 279:180-187; ; Gonzalez R., et al. (2008) Metab. Eng. 10:234-245

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. Phosphate-Buffered Saline (pH 7.4) 10% glycerol

Enzymes & Proteases

NP_418380

P0A9S5

E.coli

MGSSHHHHHH SSGLVPRGSH MGSMDRIIQS PGKYIQGADV INRLGEYLKP LAERWLVVGD KFVLGFAQST VEKSFKDAGL VVEIAPFGGE CSQNEIDRLR GIAETAQCGA ILGIGGGKTL DTAKALAHFM GVPVAIAPTI ASTDAPCSAL SVIYTDEGEF DRYLLLPNNP NMVIVDTKIV AGAPARLLAA GIGDALATWF EARACSRSGA TTMAGGKCTQ AALALAELCY NTLLEEGEKA MLAAEQHVVT PALERVIEAN TYLSGVGFES GGLAAAHAVH NGLTAIPDAH HYYHGEKVAF GTLTQLVLEN APVEEIETVA ALSHAVGLPI TLAQLDIKED VPAKMRIVAE AACAEGETIH NMPGGATPDQ VYAALLVADQ YGQRFLQEWE