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In the E. coli expression system, the recombinant human glucose-6-phosphatase (G6PC) with an N-terminal 6xHis-SUMO-tag is synthesized by cloning the gene fragment encoding the 82-117aa of the human G6PC protein into a suitable expression vector. The N-terminal 6xHis-SUMO-tag is also inserted into the vector downstream of the desired gene fragment. The constructed recombinant plasmid is introduced into E. coli host cells through a transformation process. The transformed cells are selected using appropriate markers, ensuring the presence of the recombinant plasmid. Subsequently, the transformed E. coli cells are cultured in a growth medium optimized for protein expression. Induction of protein expression is achieved by adding an inducer molecule, such as IPTG. Following an incubation period, the cells are harvested and lysed to release the intracellular contents containing the expressed recombinant G6PC protein. The purified recombinant human G6PC protein exhibits a purity level of up to 85% as determined by SDS-PAGE analysis. On the gel, the protein migrates as a band with a molecular weight of approximately 20 kDa.
In the E. coli expression system, the recombinant human glucose-6-phosphatase (G6PC) with an N-terminal 6xHis-SUMO-tag is synthesized by cloning the gene fragment encoding the 82-117aa of the human G6PC protein into a suitable expression vector. The N-terminal 6xHis-SUMO-tag is also inserted into the vector downstream of the desired gene fragment. The constructed recombinant plasmid is introduced into E. coli host cells through a transformation process. The transformed cells are selected using appropriate markers, ensuring the presence of the recombinant plasmid. Subsequently, the transformed E. coli cells are cultured in a growth medium optimized for protein expression. Induction of protein expression is achieved by adding an inducer molecule, such as IPTG. Following an incubation period, the cells are harvested and lysed to release the intracellular contents containing the expressed recombinant G6PC protein. The purified recombinant human G6PC protein exhibits a purity level of up to 85% as determined by SDS-PAGE analysis. On the gel, the protein migrates as a band with a molecular weight of approximately 20 kDa.
| Cat.No | ACP01224 | Target Name | G6PC1 |
|---|---|---|---|
| Target Synonyms | (Glucose-6-phosphatase)(G-6-Pase)(G6Pase)(Glucose-6-phosphatase alpha)(G6Pase-alpha) | Form | Liquid or Lyophilized powder |
| Expression System | E.coli | Expression Range | 82-117aa |
| Mol Weight | 17.1 kDa | Protein Length | Partial |
| Purity | Greater than 85% as determined by SDS-PAGE. | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P35575 |
|---|
Uniprot Id
P35575
Target Species
Human
Target Name
G6PC1
Target Full Name
Glucose-6-phosphatase catalytic subunit 1
Target Function
Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels.
Target Involvement
Glycogen storage disease 1A (GSD1A)
Target Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Target Protein Families
Glucose-6-phosphatase family
Target Research Area
Cancer
Target Synonyms
AW107337; G-6-Pase; G6Pase; G6Pase-alpha; g6pc; G6PC_HUMAN; G6PT; Glucose-6-phosphatase alpha; Glucose-6-phosphatase; glucose-6-phosphatase; catalytic subunit; GSD1; GSD1a; MGC163350; MGC93613; RP23-281C18.19
Target Background
Glucose-6-phosphatase (G6Pase) is a multi-subunit integral membrane protein of the endoplasmic reticulum that is composed of a catalytic subunit and transporters for G6P, inorganic phosphate, and glucose. This gene (G6PC) is one of the three glucose-6-phosphatase catalytic-subunit-encoding genes in human: G6PC, G6PC2 and G6PC3. Glucose-6-phosphatase catalyzes the hydrolysis of D-glucose 6-phosphate to D-glucose and orthophosphate and is a key enzyme in glucose homeostasis, functioning in gluconeogenesis and glycogenolysis. Mutations in this gene cause glycogen storage disease type I (GSD1). This disease, also known as von Gierke disease, is a metabolic disorder characterized by severe hypoglycemia associated with the accumulation of glycogen and fat in the liver and kidneys.
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