Recombinant E. coli Glycerol Kinase Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7849-GK

R&D Systems, part of Bio-Techne
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7849-GK-020
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Key Product Details

Source

E. coli

Accession #

AAC76908

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Glycerol Kinase Proteins and Enzymes »

Product Specifications

Source

E. coli-derived e. coli Glycerol Kinase protein
Met1-Glu502, with a C-terminal 6-His tag

Purity

>75%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Thr2

Predicted Molecular Mass

57 kDa

SDS-PAGE

52-55 kDa, reducing conditions

Activity

Measured by its ability to transfer phosphate from ATP to glycerol.
The specific activity is >1,500 pmol/min/μg, as measured under the described conditions.

Reviewed Applications

Read 1 review rated 4 using 7849-GK in the following applications:

Formulation, Preparation and Storage

7849-GK
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl, Glycerol, Brij-35 and DTT.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: Glycerol Kinase

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 (1). In the presence of glycerol, glpK is stimulated by interaction with the membrane-bound glycerol facilitator (2). In the presence of glucose, glpK activity is allosterically inhibited by fructose-1,6-bisphosphate (FBP) of the glycolytic pathway (3). 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 (4). glpK is also inhibited by phosphocarrier protein IIAGlc by a regulatory mechanism distinct from that of FBP (5). 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 (6).

References

  1. Pettigrew, D.W. et al. (1988) J. Biol. Chem. 263: 135.
  2. Voegele, R.T. et al. (1993) J. Bacteriol. 175:1087.
  3. Applebee, M.K. et al. (2011) J. Biol. Chem. 286: 23150.
  4. Hurley, J.H. et al. (1993) Science 259:673.
  5. Feese, M.D. et al. (1998) Structure 6:1407.
  6. Wu, Z.L. (2011) PLoS ONE 6(8): e23172.

Alternate Names

GK, GK1, GKD, glpK, Glycerokinase

Entrez Gene IDs

2710 (Human); 14933 (Mouse); 948423 (E. coli)

Gene Symbol

GK

UniProt

AAC76908

Additional Glycerol Kinase Products

Product Documents for Recombinant E. coli Glycerol Kinase Protein, CF

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Product Specific Notices for Recombinant E. coli Glycerol Kinase Protein, CF

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