Description
Recombinant Active Glycerol kinase Protein (His Tag) | PKSQ500004 | Gentaur US, UK & Europe Disrtribition
Synonyms: GK, glpK
Active Protein: Active protein
Activity: A DNA sequence encoding the Escherichia coli Glycerol kinase (2T-502E) was expressed with a polyhistidine tag at the N-terminus and C-terminus.
Protein Construction: A DNA sequence encoding the Escherichia coli Glycerol kinase (2T-502E) was expressed with a polyhistidine tag at the N-terminus and C-terminus.
Fusion Tag: N/C-His
Species: Escherichia coli (strain K12)
Expressed Host: E.coli
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 90 % as determined by reducing SDS-PAGE.
Endotoxin: Please contact us for more information.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 56.1kDa
Formulation: Lyophilized from sterile potassium phosphate, pH 7.4
Reconstitution: Please refer to the printed manual for detailed information.
Background: Glycerol kinase from E. coli (glpK) catalyzes the ATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate (G3P), the first and rate-limiting step in the utilization of glycerol. In the presence of glycerol, glpK is stimulated by interaction with the membrane-bound glycerol facilitator. In the presence of glucose, glpK activity is allosterically inhibited by fructose-1, 6-bisphosphate (FBP) of the glycolytic pathway. Under physiological conditions, the enzyme is in an equilibrium between the active dimer and the inactive tetramer. FBP binds to and stabilizes the inactive form, therefore shifting the usage of glycerol metabolic pathway to glycolytic pathway. GlpK is a member of a superfamily of ATPases that includes actin, hexokinase and the heat shock protein hsc70. Although these proteins are dissimilar in amino acid sequence and function, they share similar tertiary folds and likely the same catalytic mechanism. The enzyme activity was measured using a phosphatase-coupled kinase assay.
Research Area: N/A
