Recombinant Human Glucose-6-Phosphatase (G6PC1) Protein (His-SUMO)

Name: Recombinant Human Glucose-6-Phosphatase (G6PC1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-00740P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Glucose-6-Phosphatase (G6PC1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P35575
Target Symbol	G6PC1
Synonyms	(Glucose-6-phosphatase)(G-6-Pase)(G6Pase)(Glucose-6-phosphatase alpha)(G6Pase-alpha)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	QRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPS
Expression Range	82-117aa
Protein Length	Partial
Mol. Weight	17.1 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

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.
Subcellular Location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Protein Families	Glucose-6-phosphatase family
Database References	HGNC: 4056 OMIM: 232200 KEGG: hsa:2538 STRING: 9606.ENSP00000253801 UniGene: PMID: 28829278 3'-UTR SNP rs2229611 in G6PC1 affects mRNA stability, expression and Glycogen Storage Disease type-Ia risk PMID: 28502559 crystal structures of the FoxO1 DNA binding domain in complex with the G6PC1 promoter PMID: 28223045 Notch1 expression is reduced and glucose-6-phosphatase and perilipin-5 (G6PC/PLIN5) are upregulated in liver biopsies from nonalcoholic steatohepatitis (NASH) and nonalcoholic fatty liver disease (NAFLD) patients. PMID: 27428080 Mutation analysis of the G6PC gene revealed that GSD Ia accounted for 11% in GSD patients with involvement of liver. Three patients were homozygous for R83C mutation. In addition, a novel stop mutation, Y85X, was identified in a patient with the typical features of GSD Ia. PMID: 28360385 Post-translational regulation of the glucose-6-phosphatase complex by cyclic AMP is a crucial determinant of endogenous glucose production and is controlled by the glucose-6-phosphate transporter. PMID: 26958868 ApoA-IV colocalizes with NR4A1, which suppresses G6Pase and PEPCK gene expression at the transcriptional level, reducing hepatic glucose output and lowering blood glucose. PMID: 26556724 By direct DNA sequencing, three novel G6PC variations were identified which expanded the G6PC mutation spectrum, and provided conclusive genetic evidences for the definitive diagnosis of the Chinese patients. PMID: 24980439 This study is the first to demonstrate a functional relationship between the critical gluconeogenic and glycogenolytic enzyme G6PC with the metabolic adaptations during glioblastoma invasion. PMID: 25001192 The spectrum of mutations in the G6PC gene. PMID: 24355556 Lipopolysaccharide and monophosphoryl lipid A also up-regulated G6PC and PCK1 transcript abundance in a TLR4-dependent manner. PMID: 23465595 Both GSD-1a and G6PT strongly colocalised in perinuclear membranes. showed that GSD1 mutations did neither alter the G6PC or G6PT chimera localisation, nor the interaction between G6PT termini. PMID: 21983240 results reveal a novel link between glucose metabolism and the DNA damage signaling pathway and suggest a possible role for PEPCK and G6P in the DNA damage response PMID: 21733854 data mitigate against G6PD deficiency contributing to stroke risk in individuals with sickle cell anemia. PMID: 21328436 description of G6PC mutations in Thailand patients with glycogen storage disease type Ia PMID: 19832742 we report the results of structure and function studies of the 48 missense mutations and the DeltaF327 codon deletion mutation, grouped as active site, helical, and nonhelical mutations PMID: 11739393 active site of G6Pase: role of HIS176 as the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis PMID: 12093795 homozygosity for one G6PC mutation, G188R, seems to be associated with a glycogen storage disease type I non-a phenotype and homozygosity for the 727G>T mutation may be associated with a milder phenotype but an increased risk for hepatocellular carcinoma PMID: 12373566 The amino-terminal domain of G6PT is required for optimal glucose-6-phosphate uptake activity. PMID: 12444104 maximum repression of basal glucose-6-phosphatase catalytic subunit (G6Pase) gene transcription by insulin requires two distinct promoter regions, designated that together form an insulin response unit. PMID: 12556524 Five mutants lack microsomal G6P uptake activity and one retains residual activity, suggesting that in G6PT the signature motif is a functional element required for microsomal glucose-6-phosphate transport. PMID: 12560945 a novel, widely expressed G6Pase-related protein, PAP2.8/UGRP, renamed here G6Pase-beta couples with the G6P transporter to form an active G6Pase complex that can hydrolyze G6P to glucose PMID: 13129915 Glc-6-Pase-alpha and Glc-6-Pase-beta share a similar active site structure, topology, and mechanism of action PMID: 14718531 G6pc expression was functionally silenced by adenovirus-mediated delivery of short hairpin RNA. PMID: 14759518 Findings suggest that the screening for 727G-->T and R83H mutations of glucose-6-phosphatase gene in conjunction with the 1176 polymorphism linkage analysis is a good method for gene and prenatal diagnosis of glycogen storage disease Ia. PMID: 15696478 HNF4alpha, CREM, HNF1alpha, and C/EBPalpha have roles in transcriptional regulation of the glucose-6-phosphatase gene by cAMP/vasoactive intestinal peptide in the intestine PMID: 16893891 G6PC1 hepatic activity was abnormally low in 98 SIDS (preterm, n=13; term, n=85), and non-SIDS preterm infants (n=35) compared to term non-SIDS infants (n=29) and adults (n=9) PMID: 17354259 analysis of mutation spectrum of glycogen storage disease type Ia in Tunisia PMID: 18008183 summary of the reported G6PC mutations and review what mutagenesis studies have revealed about the structure and function of the G6PC catalytic unit [review] PMID: 18449899 EGF also inhibits hepatic G6Pase gene expression in vivo PMID: 18847435 Identification of a risk conferring single nucleotide polymorphism in G6PC for type 2 diabetes in a Chinese population. PMID: 19082990 Increased transcriptional expression of PEPCK1 and G6Pc does not account for increased gluconeogenesis and fasting hyperglycemia in patients with type 2 diabetes mellitus. PMID: 19587243

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.