-
Chinese (Simplified)
-
English
-
German
-
Korean
-
Spanish
Chinese (Simplified)
English
German
Korean
Spanish
Sign up for an account to enjoy easy online shopping and instant order tracking.
The generation process of the recombinant human glucose-6-phosphatase (G6PC) involves ligating a gene fragment encoding amino acids 82 to 117 of the human G6PC protein with an N-terminal 6xHis-sumostar-tag. This fusion construct is carefully cloned into an appropriate expression vector. Subsequently, the recombinant vector is introduced into the yeast expression system, enabling the efficient expression of the desired recombinant human G6PC protein. Upon successful expression, the recombinant G6PC protein is extracted and purified from the yeast cell lysate, achieving a purity level of over 90% as confirmed by SDS-PAGE analysis. G6PC, an essential enzyme involved in glucose metabolism, has also been linked to cancer, playing a critical role in regulating glucose homeostasis within cancer cells.
The generation process of the recombinant human glucose-6-phosphatase (G6PC) involves ligating a gene fragment encoding amino acids 82 to 117 of the human G6PC protein with an N-terminal 6xHis-sumostar-tag. This fusion construct is carefully cloned into an appropriate expression vector. Subsequently, the recombinant vector is introduced into the yeast expression system, enabling the efficient expression of the desired recombinant human G6PC protein. Upon successful expression, the recombinant G6PC protein is extracted and purified from the yeast cell lysate, achieving a purity level of over 90% as confirmed by SDS-PAGE analysis. G6PC, an essential enzyme involved in glucose metabolism, has also been linked to cancer, playing a critical role in regulating glucose homeostasis within cancer cells.
| Cat.No | ACP01137 | 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 | Yeast | Expression Range | 82-117aa |
| Mol Weight | 17.5 kDa | Protein Length | Partial |
| Purity | Greater than 90% 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.
Notification