Analytical Data
-
Gene name
glpK
- Application
-
Alternative Names
glpK;Glycerol kinase
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0A6F3
-
Expression Region
2-502aa
-
AA Sequence
TEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPISGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEHDE
-
Molecular Weight
60.1kDa
-
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
Glucose-6-phosphate kinase (glpK) is an essential enzyme involved in the regulation of glucose metabolism, particularly in the glycolytic pathway. It catalyzes the phosphorylation of glucose-6-phosphate, playing a critical role in energy production and metabolic control in various organisms, including bacteria, plants, and animals. Research on glpK has gained significance due to its potential applications in biotechnology and medicine, such as its role in metabolic engineering, the development of antimicrobial agents, and understanding metabolic disorders. The recombinant production of glpK allows for the detailed study of its structure, function, and regulation, enabling researchers to explore how alterations in this enzyme can affect metabolic pathways. Furthermore, the availability of large quantities of pure glpK protein facilitates crystallographic studies, which can provide insights into its active site and interaction with substrates or inhibitors. As metabolic diseases and antibiotic resistance continue to pose significant public health challenges, understanding glpK function and its regulatory mechanisms could lead to novel therapeutic strategies and expanded applications in metabolic engineering for biofuel production and bioremediation. Thus, the research on glpK recombinant protein not only enhances our fundamental knowledge of metabolic processes but also holds promise for practical applications across multiple fields.
