Purity
Greater than 85% as determined by SDS-PAGE.
Alternative Names
(Glucose-6-phosphatase)(G-6-Pase)(G6Pase)(Glucose-6-phosphatase alpha)(G6Pase-alpha)
Species
Homo sapiens (Human)
Expression Region
82-117aa
Target Protein Sequence
QRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPS
Note: The complete sequence including tag
sequence, target protein sequence and linker sequence could be provided upon request.
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that
we have in stock, however, if you have any special requirement for the format, please remark your
requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw
cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature
and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized
form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description
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.