Analytical Data
-
Gene name
Polyphosphate glucokinase
- Application
-
Alternative Names
Thermobifida fusca (strain YX); Kinase; Transferase
-
Species
Others
-
Source
E. coli
-
Tag
Tag Free
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q47NX5
-
Expression Region
M1-A262
-
Protein Length
Full Length
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Polyphosphate glucokinase (PPGK) is an enzyme that catalyzes the phosphorylation of glucose using polyphosphate as a phosphate donor, playing a critical role in microbial energy metabolism and stress responses. The study of PPGK has gained traction due to its potential applications in bioengineering and biotechnology, particularly in the production of biofuels and biochemicals. Understanding the structure and function of PPGK can provide insights into the regulation of glucose metabolism in various organisms, including bacteria and eukaryotes. Recent advancements in recombinant DNA technology have facilitated the expression and purification of PPGK from different sources, allowing researchers to investigate its enzymatic properties and regulatory mechanisms. This research can offer avenues for metabolic engineering, where PPGK could be utilized to enhance microbial fermentation processes or to develop novel biocatalysts with improved efficiency. Given the rising interest in sustainable energy sources, PPGK represents a promising target for developing innovative biotechnological solutions that leverage microbial metabolism for commercial applications.
