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

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

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

Pck1

Uniprot NO.

P07379

Species

Rattus norvegicus (Rat)

Source

Yeast

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
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full length protein

Tag Info

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.

Storage

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

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.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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

Peroxynitrite-induced coronary vascular dysfunction may be mediated, at least in part, through increased expressions and activities of RhoA, ROCK1, and ROCK2. PMID:27724862
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
PEPCK is downregulated and has a role in reduction of blood glucose and gluconeogenesis after phenobarbital administration in rats PMID:26348778
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
Leptin activates NOS III and induces nitric oxide that nitrates PEPCK-C to reduce its level and glyceroneogenesis. PMID:22808220
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
retinoic acid response element 2 in rat Pck1 promoter is responsible for transcriptional activation by retinoic acid PMID:21519922
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
Pck1 plays an important role in both the mammary gland adipocytes and epithelial cells during lactation PMID:21504969
During acute hepatic failure severe endotoxemia damages the function of gluconeogenesis in livers and kidneys by inhibiting transcription of PEPCK. PMID:17903369
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
Expression of the PEPCK gene in H4IIEC3 rat hepatoma cells is closely coordinated with cell proliferation. PMID:11820793
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
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
promoter context may influence which domains within a transcription factor are employed to mediate transactivation of PEPCK PMID:12237288
transcription of the gene for phosphoenolpyruvate carboxykinase (GTP) in the liver is regulated by SREBP-1c and Sp1 PMID:14744869
PEPCK transcription induced by protein kinase A is regulated by CREB and C/EBP. PMID:15604115
SHARP-2 is a potential repressor of PEPCK gene expression PMID:15733865
Hepatic PEPCK gene expression is modulated by chronic exercise training. PMID:16458327
Pck1 is up-regulated during liver gluconeogenesis. PMID:17158265
Endogenous lipid molecules induce PEPCK-C gene transcription and attenuate insulin action in liver. PMID:17678617
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
Suppression of phosphoenolpyruvate carboxykinase gene expression by reduced endogenous glutathione level PMID:17964299
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
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
skeletal muscle PEPCK has a role in determining physical activity levels PMID:19521512
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
In white adipose tissue, overexpression causes obesity without diabetes, while underexpression causes lipodystrophy and perhaps insulin resistance. PMID:12409311
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
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
The first cAMP response element (CRE) was discovered upstream of the rat PEPCK gene. PMID:3015903
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