e.coli gldA protein (Recombinant) (His-Tag) (STJP019194)

SPECIFICATIONS
HostE.coli
ImmunogenE.coli
STJP019194
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General Information

Short DescriptionRecombinant-e.coli gldA-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications.
ApplicationsEnzyme Activity/SDS-PAGE
HostE.coli
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

Concentration1 mg/mL
FormulationLiquid in phosphate-Buffered Saline (pH 7.4) 10% Glycerol
Storage InstructionFor short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles.
ImmunoreactivitySpecific activity: > 14 Units/ml One unit will oxidize 1.0 umole of glycerol to dihydroxyacetone per minute at pH 8.0 at 25C

Target Information

Accession NumberNP_418380
ImmunogenE.coli
Immunogen Region1-367aa
Immunogen SequenceMGSSHHHHHH SSGLVPRGSH MGSMDRIIQS PGKYIQGADV INRLGEYLKP LAERWLVVGD KFVLGFAQST VEKSFKDAGL VVEIAPFGGE CSQNEIDRLR GIAETAQCGA ILGIGGGKTL DTAKALAHFM GVPVAIAPTI ASTDAPCSAL SVIYTDEGEF DRYLLLPNNP NMVIVDTKIV AGAPARLLAA GIGDALATWF EARACSRSGA TTMAGGKCTQ AALALAEL

Additional Info

Background 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.

Information sourced from Uniprot.org

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