Recombinant Rat Phosphoenolpyruvate carboxykinase, cytosolic [GTP](Pck1)

Code CSB-YP017613RA
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Source Yeast
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Code CSB-EP017613RA
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Source E.coli
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Code CSB-EP017613RA-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-BP017613RA
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Source Baculovirus
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Code CSB-MP017613RA
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Pck1
Uniprot No. P07379
Alternative Names Pck1; Phosphoenolpyruvate carboxykinase; cytosolic [GTP]; PEPCK-C; EC 4.1.1.32
Species Rattus norvegicus (Rat)
Expression Region 1-622
Target Protein Sequence MPPQLHNGLD FSAKVIQGSL DSLPQEVRKF VEGNAQLCQP EYIHICDGSE EEYGRLLAHM QEEGVIRKLK KYDNCWLALT DPRDVARIES KTVIITQEQR DTVPIPKSGQ SQLGRWMSEE DFEKAFNARF PGCMKGRTMY VIPFSMGPLG SPLAKIGIEL TDSPYVVASM RIMTRMGTSV LEALGDGEFI KCLHSVGCPL PLKKPLVNNW ACNPELTLIA HLPDRREIIS FGSGYGGNSL LGKKCFALRI ASRLAKEEGW LAEHMLILGI TNPEGKKKYL AAAFPSACGK TNLAMMNPTL PGWKVECVGD DIAWMKFDAQ GNLRAINPEN GFFGVAPGTS VKTNPNAIKT IQKNTIFTNV AETSDGGVYW EGIDEPLAPG VTITSWKNKE WRPQDEEPCA HPNSRFCTPA SQCPIIDPAW ESPEGVPIEG IIFGGRRPAG VPLVYEALSW QHGVFVGAAM RSEATAAAEH KGKVIMHDPF AMRPFFGYNF GKYLAHWLSM AHRPAAKLPK IFHVNWFRKD KNGKFLWPGF GENSRVLEWM FGRIEGEDSA KLTPIGYVPK EDALNLKGLG DVNVEELFGI SKEFWEKEVE EIDKYLEDQV NADLPYEIER ELRALKQRIS QM
Protein Length Full length protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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
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.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°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 Data

Function Catalyzes the conversion of oxaloacetate (OAA) 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.
Gene References into Functions
  1. Peroxynitrite-induced coronary vascular dysfunction may be mediated, at least in part, through increased expressions and activities of RhoA, ROCK1, and ROCK2. PMID: 27724862
  2. GBS can reduce blood glucose in T2DM rats while improving glucose tolerance and hyperglycemia, and the mechanism appears to be associated with a decrease of hepatic PEPCK mRNA and protein expression. PMID: 26681041
  3. PEPCK is downregulated and has a role in reduction of blood glucose and gluconeogenesis after phenobarbital administration in rats PMID: 26348778
  4. It observed lower expression of hepatic PEPCK mRNA, in the magnesium-deficient rats, thus suggesting a possible compensatory mechanism to diminish glycogenesis. A low-magnesium diet alters glucocorticoid metabolism, which leads to endothelial damage. PMID: 23015202
  5. Leptin activates NOS III and induces nitric oxide that nitrates PEPCK-C to reduce its level and glyceroneogenesis. PMID: 22808220
  6. The increase of protein intake during pregnancy could decrease the expression of y acid synthetase and PEPCK mRNA, and prevent offspring from high-fat diet-induced obesity in adult. PMID: 19548567
  7. retinoic acid response element 2 in rat Pck1 promoter is responsible for transcriptional activation by retinoic acid PMID: 21519922
  8. In addition to increased transcription rate, a gestational high fat diet resulted in modifications of the Pck1 histone code in livers of offspring. PMID: 21486814
  9. Pck1 plays an important role in both the mammary gland adipocytes and epithelial cells during lactation PMID: 21504969
  10. During acute hepatic failure severe endotoxemia damages the function of gluconeogenesis in livers and kidneys by inhibiting transcription of PEPCK. PMID: 17903369
  11. Taken together, our results suggest that, during very demanding exercise, muscle-derived interleukin-6 could help increase hepatic glucose production by directly upregulating PEPCK mRNA abundance. PMID: 19850730
  12. Expression of the PEPCK gene in H4IIEC3 rat hepatoma cells is closely coordinated with cell proliferation. PMID: 11820793
  13. increased PEPCK gene transcription at acid pH required a cis-acting element (enhancer) in the more distal 5' flanking region of the promoter PMID: 11939717
  14. polyunsaturated and nonmetabolized FAs stimulate adipose PEPCK, therefore potentially enhancing glyceroneogenesis and reducing FA output. This mechanism could participate in the hypolipidemic action of PUFAs. PMID: 11968005
  15. promoter context may influence which domains within a transcription factor are employed to mediate transactivation of PEPCK PMID: 12237288
  16. transcription of the gene for phosphoenolpyruvate carboxykinase (GTP) in the liver is regulated by SREBP-1c and Sp1 PMID: 14744869
  17. PEPCK transcription induced by protein kinase A is regulated by CREB and C/EBP. PMID: 15604115
  18. SHARP-2 is a potential repressor of PEPCK gene expression PMID: 15733865
  19. Hepatic PEPCK gene expression is modulated by chronic exercise training. PMID: 16458327
  20. Pck1 is up-regulated during liver gluconeogenesis. PMID: 17158265
  21. Endogenous lipid molecules induce PEPCK-C gene transcription and attenuate insulin action in liver. PMID: 17678617
  22. Comparison of the Mn2+-OAA-Mn2+GDP and Mn2+-Mn2+GTP structures illustrates a marked difference in the bound conformations of the nucleotide substrates in which the GTP nucleotide is bound in a high-energy state. PMID: 17685635
  23. Suppression of phosphoenolpyruvate carboxykinase gene expression by reduced endogenous glutathione level PMID: 17964299
  24. 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
  25. structural data are consistent with a model in that the energy input from substrate association results in changes in the free energy landscape for the protein, allowing for structural transitions along an induced fit pathway PMID: 18772387
  26. skeletal muscle PEPCK has a role in determining physical activity levels PMID: 19521512
  27. Expression of the rat PEPCK gene in adipose tissue requires a PPAR-gamma/RXR binding site located 1 kbp upstream of the promoter. Similar elements are in the human and mouse gene. PMID: 10224131
  28. In white adipose tissue, overexpression causes obesity without diabetes, while underexpression causes lipodystrophy and perhaps insulin resistance. PMID: 12409311
  29. PEPCK catalyzes a key step of gluconeogenesis and glyceroneogenesis. It is expressed at significant levels in liver, kidney, intestine, white and brown adipose tissues, and lactating mammary gland. Control is mainly at transcription. PMID: 9242918
  30. PEPCK is a key enzyme of glyceroneogenesis in adipocytes and hepatocytes. Glyceroneogenesis produces glycerol-3-P to control the triglyceride/fatty acid cycle. PMID: 12788931
  31. The first cAMP response element (CRE) was discovered upstream of the rat PEPCK gene. PMID: 3015903
  32. Expression of the rat PEPCK gene in adipose tissue requires a PPAR-gamma/RXR binding site located 1 kbp upstream of the promoter. Similar elements are in the human and mouse gene. PMID: 10224131

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Subcellular Location Cytoplasm
Protein Families Phosphoenolpyruvate carboxykinase [GTP] family
Database Links

KEGG: rno:362282

STRING: 10116.ENSRNOP00000030913

UniGene: Rn.104376

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