IDNK E.Coli, Active
Escherichia Coli.
Thermosensitive gluconokinase, Gluconate kinase 1, idnK, D-gluconate kinase thermosensitive, D-gluconate kinase, thermosensitive, ECK4261, gntV, JW4225, b4268
Greater than 90.0% as determined by SDS-PAGE.
Description
IDNK Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187) and having a molecular mass of 23.4 kDa.
IDNK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
The enzyme D-gluconate kinase, also known as idnk, is a temperature-sensitive protein belonging to the gluconokinase gntK/gntV protein family. It consists of 187 amino acids. Idnk plays a role in catalyzing the conversion of ATP and D-gluconate into ADP and 6-phospho-D-gluconate. Notably, idnk is involved in sex determination, and deletion of a specific region on chromosome 9p can lead to sex reversal from male to female, resulting in a female with an XY genotype.
Recombinant IDNK, expressed in E.Coli, is a single, non-glycosylated polypeptide chain. It consists of 210 amino acids, including a 23 amino acid His-Tag at the N-terminus, and has a molecular weight of 23.4 kDa. The protein is purified using proprietary chromatographic techniques.
The IDNK solution is provided at a concentration of 1 mg/ml and contains 10% glycerol, 1mM DTT, 0.15M NaCl, and 20mM Tris-HCl buffer (pH 8.0).
The purity of IDNK is greater than 90%, as determined by SDS-PAGE analysis.
The specific activity of IDNK is greater than 80 units/mg. One unit of activity is defined as the amount of enzyme required to catalyze the conversion of 1.0 micromole of D-gluconate to 6-phospho-D-gluconate per minute at pH 8.0 and a temperature of 37°C.
Thermosensitive gluconokinase, Gluconate kinase 1, idnK, D-gluconate kinase thermosensitive, D-gluconate kinase, thermosensitive, ECK4261, gntV, JW4225, b4268
Escherichia Coli.
MGSSHHHHHH SSGLVPRGSH MGSMAGESFI LMGVSGSGKT LIGSKVAALL SAKFIDGDDL HPAKNIDKMS QGIPLSDEDR LPWLERLNDA SYSLYKKNET GFIVCSSLKK QYRDILRKGS PHVHFLWLDG DYETILARMQ RRAGHFMPVA LLKSQFEALE RPQADEQDIV RIDINHDIAN VTEQCRQAVL AIRQNRICAK EGSASDQRCE
Product Science Overview
The thermosensitive gluconokinase from E. coli is a recombinant protein that is produced in E. coli cells. It is a single, non-glycosylated polypeptide chain consisting of 210 amino acids, with a molecular mass of approximately 23.4 kDa . The protein is fused to a 23 amino acid His-tag at the N-terminus, which facilitates its purification using chromatographic techniques .
The enzyme is termed “thermosensitive” because its activity is influenced by temperature. This property is particularly useful in research and industrial applications where temperature control is crucial.
The recombinant thermosensitive gluconokinase is expressed in E. coli and purified to a high degree of purity, typically greater than 95%, as determined by SDS-PAGE . The protein is formulated in a sterile, filtered colorless solution containing 20 mM Tris-HCl buffer (pH 8.0), 0.15 M NaCl, 10% glycerol, and 1 mM DTT . This formulation helps maintain the stability and activity of the enzyme.
Thermosensitive gluconokinase has several applications in biochemical research and industrial processes:
- Metabolic Engineering: It is used in the study of metabolic pathways involving gluconate and its derivatives. By manipulating the expression of this enzyme, researchers can investigate the effects on the overall metabolic flux.
- Biocatalysis: The enzyme can be used in biocatalytic processes to produce 6-phosphogluconate, which is a valuable intermediate in various biochemical pathways.
- Protein Engineering: The thermosensitive nature of the enzyme makes it an interesting target for protein engineering studies aimed at understanding and improving enzyme stability and activity at different temperatures.
For short-term storage, the enzyme can be kept at 4°C if it will be used within 2-4 weeks. For longer-term storage, it is recommended to store the enzyme at -20°C, with the addition of a carrier protein such as 0.1% HSA or BSA to prevent degradation . It is important to avoid multiple freeze-thaw cycles to maintain the enzyme’s activity and stability.
