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Recombinant E.coli Glycerol kinase Protein (His Tag)
SKU: PDEO100001-100
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Recombinant E.coli Glycerol kinase Protein (His Tag)
| SKU # | PDEO100001 |
| Expression Host | E. coli |
Description
| Synonyms | GK;glpK |
| Species | E.coli |
| Expression_host | E.coli |
| Sequence | Thr2-Glu502 |
| Accession | P0A6F3 |
| Mol_Mass | 56.1 kDa |
| AP_Mol_Mass | 55-58 kDa |
| Tag | N-His & C-His |
| Bio_Activity | Not validated for activity |
Properties
| Purity | > 90 % as determined by reducing SDS-PAGE. |
| Endotoxin level | Please contact us for more information. |
| 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. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis |
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.