Recombinant Human Phosphoenolpyruvate carboxykinase, cytosolic [GTP](PCK1)

Code CSB-YP017613HU
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Source Yeast
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Code CSB-EP017613HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP017613HU
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Source Baculovirus
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Code CSB-MP017613HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names PCK1
Uniprot No. P35558
Alternative Names cytosolic [GTP]; GTP; PCK1; PCKGC_HUMAN; PEP carboxykinase; PEPCK-C; PEPCK1; PEPCKC; Phosphoenolpyruvate carboxykinase 1 (soluble); Phosphoenolpyruvate carboxykinase 1; Phosphoenolpyruvate carboxykinase; Phosphoenolpyruvate carboxykinase, cytosolic [GTP]; Phosphoenolpyruvate carboxykinase, cytosolic; Phosphoenolpyruvate carboxylase; Phosphopyruvate carboxylase
Species Homo sapiens (Human)
Expression Region 1-622
Protein Length Full length protein
Tag Info The following tags are available.
N-terminal His-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form 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 before Lyophilization 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.
and FAQs
Protein FAQs
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 Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis. Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle. At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate. Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis. The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis. In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor. The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes.
Gene References into Functions
  1. This study reveals a unique mechanism to suppress hepatocellular carcinoma by switching from glycolysis to gluconeogenesis through Nur77 antagonism of PEPCK1 degradation. PMID: 28240261
  2. circC3P1 acts as a tumor suppressor via enhancing PCK1 expression by sponging miR-4641 in hepatocellular carcinoma. PMID: 29608893
  3. The expression levels of PCK1 were suppressed in hepatocellular carcinoma (HCC) samples and in cells derived from HCC tissues. PMID: 29768256
  4. Study investigated the molecular basis of such effects focusing on a commonly studied polymorphism in pig Pgc1alpha, which changes a cysteine at position 430 (WT) of the protein to a serine (C430S); found that differential O-GlcNAcylation of Pgc1alpha regulates PCK1 activity and this molecular mechanism could explain at least in part the epistatic interaction between both genes. PMID: 28644880
  5. Study identified a novel homozygous PCK1 missense mutation causing cytosolic phosphoenolpyruvate carboxykinase deficiency presenting as childhood hypoglycemia. PMID: 28216384
  6. HBXIP is able to depress the gluconeogenesis in hepatoma cells by suppressing PCK1 to promote hepatocarcinogenesis, involving miR-135a/FOXO1 axis and PI3K/Akt/p-FOXO1 pathway. PMID: 27609066
  7. an extended binding site in the catalytic cleft of cPEPCK which is used by 3-MPA to inhibit cPEPCK non-competitively. PMID: 26528723
  8. A mutation of PCK1 associated with Smith-Magenis Syndrome, cytosolic PEPCK deficiency and NMDA receptor glutamate insensitivity. PMID: 24863970
  9. Insulin-dependent translocation of FOXO1 regulated transcriptional repression of PCK1 concomitant with the formation of the FOXO1-euchromatic histone-lysine N-methyltransferase2 (EHMT2) complex and histone modifications of the PCK1 promoter region PMID: 25736587
  10. Lipopolysaccharide and monophosphoryl lipid A also up-regulated G6PC and PCK1 transcript abundance in a TLR4-dependent manner. PMID: 23465595
  11. The PCK1 tag-single nucleotide polymorphisms influenced insulin resistance by interacting with plasma n-3 polyunsaturated fatty acids levels in metabolic syndrome patients. PMID: 23092637
  12. HCV core protein expression-mediated FOXO1 activation and the increased PGC-1alpha leaded to the elevation of PCK1 at the mRNA level PMID: 22489460
  13. Acetylation regulates the stability of the gluconeogenic rate-limiting enzyme PEPCK1. PMID: 21726808
  14. Data show PEPCK-C and CPT-1 mRNAs are more abundant in non-tumoral tissues than in the tumoral counterpart, whereas the opposite occurred for the FAS gene. PMID: 20691246
  15. Studies demonstrate the association between PCK1 and smaller average brain volume. PMID: 21152065
  16. Study in the EYHS cohort failed to identify an association of PCK1 polymorphisms with obesity, physical activity, and fitness. PMID: 20134411
  17. crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site PMID: 11851336
  18. Conserved amino acids within CCAAT enhancer-binding proteins (C/EBP(alpha) and beta) regulate gene expression PMID: 11997389
  19. promoter context may influence which domains within a transcription factor are employed to mediate transactivation of PEPCK PMID: 12237288
  20. the PGC- 1-regulated phospho(enol)pyruvate carboxykinase (PEPCK) promoter is a novel target promoter for SHP inhibition PMID: 12324453
  21. transcription of the gene for phosphoenolpyruvate carboxykinase (GTP) in the liver is regulated by SREBP-1c and Sp1 PMID: 14744869
  22. Promoter single nucleotide polymorphism in PCK1 was resistant to down-regulation by insulin in vitro and associated with type 2 diabetes mellitus. PMID: 14764811
  23. PCK1 has been implicated as one of many genes associated with type 2 diabetes mellitus [review] PMID: 15046742
  24. AUF1 binds to multiple destabilizing elements within the 3'-UTR that participate in the rapid turnover of the phosphoenolpyruvate carboxykinase mRNA. PMID: 15951444
  25. The multiple instability elements present within the 3'-UTR may function synergistically to mediate both the rapid degradation and the cAMP-induced stabilization of PEPCK mRNA. The latter process may result from a PKA-dependent phosphorylation of AUF1. PMID: 16144962
  26. Subjects with the PCK1-232G/G genotype had more carotid IMT (0.80+/-0.02 versus 0.73+/-0.03 mm; P=0.007) but less TPV (0.10+/-0.09 versus 0.38+/-0.13; P=0.03) than subjects with other genotypes. PMID: 16282543
  27. Significant association of single nucleotide polymorphism within three genes--PPARgamma, SOS2, and PCK1--with Alzheimer's disease, was confirmed. PMID: 17440948
  28. IFN-gamma exerts a tissue-specific action in rodents and humans, having glyceroneogenesis and the PEPCK-C gene as selective targets to intensify fatty acids release from adipocytes PMID: 17495004
  29. The effects of several variants of retinoic acid on the expression and activity of PEPCK in human, mouse, and rat adipose tissue are reported. PMID: 18492826
  30. Reduced CREB phosphorylation (Ser-129) associated with inactivation of GSK3beta by Ser-9 phosphorylation may be the major mechanism underlying PEPCK-C gene suppression by AMPK-activating agents such as biguanide PMID: 18801732
  31. The aromatic ring of Tyr235 in PEPCK helps to position PEP in the active site and the hydroxyl group allows an optimal PEP-Mn(2+) distance for efficient phosphoryl transfer and overall catalysis. PMID: 19021757
  32. Val184 of PCK1 gene might increase the risk of type 2 diabetes in eastern Chinese population with BMI<23 kg/m(2) via reducing the PEPCK-C activity. PMID: 19070910
  33. Study validated a predicted SP1 binding site in the control of PCK1 transcription using gel shift and reporter assays. PMID: 19329064
  34. study is the first to investigate the association between variants of the PCK1 gene and type 2 diabetes in South Asians PMID: 19725958

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Involvement in disease Phosphoenolpyruvate carboxykinase deficiency, cytosolic (PCKDC)
Subcellular Location Cytoplasm, cytosol. Endoplasmic reticulum.
Protein Families Phosphoenolpyruvate carboxykinase [GTP] family
Tissue Specificity Major sites of expression are liver, kidney and adipocytes.
Database Links

HGNC: 8724

OMIM: 261680

KEGG: hsa:5105

STRING: 9606.ENSP00000319814

UniGene: Hs.1872

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