GLK E.coli

Glucokinase E.coli Recombinant
Cat. No.
BT10176
Source
E.coli.
Synonyms
Glucokinase, Glucose kinase, glk, b2388, JW2385.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

GLK E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a) and having a molecular mass of 37.1kDa.
GLK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glucokinase, also known as GLK, is a member of the bacterial glucokinase family. GLK is not highly significant in E. coli because glucose is already transported into the cell through the PTS system as glucose 6-phosphate.
Description
Recombinant GLK from E. coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a) and having a molecular mass of 37.1 kDa. GLK is fused to a 23 amino acid His-tag at the N-terminus and purified by proprietary chromatographic techniques.
Physical Appearance
Sterile filtered, colorless solution.
Formulation
GLK protein solution (1.0 mg/ml) in 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, and 10% glycerol.
Stability
Store at 4°C if the entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods. For long term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Purity
Greater than 95% as determined by SDS-PAGE.
Synonyms
Glucokinase, Glucose kinase, glk, b2388, JW2385.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTKYALV GDVGGTNARL ALCDIASGEI SQAKTYSGLD YPSLEAVIRV YLEEHKVEVK DGCIAIACPI TGDWVAMTNH TWAFSIAEMK KNLGFSHLEI INDFTAVSMA IPMLKKEHLI QFGGAEPVEG KPIAVYGAGT GLGVAHLVHV DKRWVSLPGE GGHVDFAPNS EEEAIILEIL RAEIGHVSAE RVLSGPGLVN LYRAIVKADN RLPENLKPKD ITERALADSC TDCRRALSLF CVIMGRFGGN LALNLGTFGG VFIAGGIVPR FLEFFKASGF RAAFEDKGRF KEYVHDIPVY LIVHDNPGLL GSGAHLRQTL GHIL.

Product Science Overview

Expression in E. coli

Recombinant glucokinase is often expressed in Escherichia coli (E. coli) due to the bacterium’s well-characterized genetics, rapid growth, and ability to express high levels of recombinant proteins . The recombinant glucokinase protein expressed in E. coli is typically used for research purposes, including studies on enzyme kinetics, glucose metabolism, and diabetes .

Structure and Function

Glucokinase has a high Km for glucose, meaning it is effective only when glucose is abundant . This property makes it a key regulator of glucose levels in the body. In pancreatic beta cells, glucokinase acts as a glucose sensor, modulating insulin secretion in response to blood glucose levels . In the liver, it facilitates the uptake and conversion of glucose, acting as an insulin-sensitive determinant of hepatic glucose usage .

Clinical Significance

Mutations in the glucokinase gene (GCK) can lead to various metabolic disorders. For instance, certain mutations are associated with non-insulin-dependent diabetes mellitus (NIDDM), maturity-onset diabetes of the young (MODY2), and persistent hyperinsulinemic hypoglycemia of infancy (PHHI) . Understanding the function and regulation of glucokinase is therefore critical for developing therapeutic strategies for these conditions.

Research Applications

Recombinant glucokinase from E. coli is widely used in research to study its biochemical properties and regulatory mechanisms . It is also employed in drug discovery efforts aimed at modulating glucokinase activity to treat diabetes and other metabolic disorders .

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