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

This Human PCK1 recombinant protein was produced in E.coli, where the gene sequence encoding Human PCK1 (1-622aa) was expressed with the N-terminal 6xHis tag. The purity of this PCK1 protein was greater than 90% by SDS-PAGE.PCK1 plays a critical role in the gluconeogenesis pathway. This pathway helps maintain blood sugar levels when they are low due to fasting or extended periods without eating. It allows liver and kidney cells to synthesize glucose from non-sugar substrates to supply to other tissues, including the brain. The activity of PCK1 is regulated by various factors, including hormones such as insulin and adrenaline, energy status, and glucose concentration. Insulin inhibits the activity of PCK1, promoting glucose uptake and storage, while stress hormones like adrenaline can stimulate PCK1 activity, increasing glucose release. PCK1 is crucial for maintaining normal blood sugar levels and energy balance. Defects or abnormal activity of PCK1 are associated with diabetes, obesity, and metabolic disorders. Due to its importance in glucose metabolism, PCK1 has become a potential drug target. Some research is exploring the possibility of regulating PCK1 activity to treat diseases related to blood sugar regulation.

ACP04294

This Human PCK1 recombinant protein was produced in E.coli, where the gene sequence encoding Human PCK1 (1-622aa) was expressed with the N-terminal 6xHis tag. The purity of this PCK1 protein was greater than 90% by SDS-PAGE.PCK1 plays a critical role in the gluconeogenesis pathway. This pathway helps maintain blood sugar levels when they are low due to fasting or extended periods without eating. It allows liver and kidney cells to synthesize glucose from non-sugar substrates to supply to other tissues, including the brain. The activity of PCK1 is regulated by various factors, including hormones such as insulin and adrenaline, energy status, and glucose concentration. Insulin inhibits the activity of PCK1, promoting glucose uptake and storage, while stress hormones like adrenaline can stimulate PCK1 activity, increasing glucose release. PCK1 is crucial for maintaining normal blood sugar levels and energy balance. Defects or abnormal activity of PCK1 are associated with diabetes, obesity, and metabolic disorders. Due to its importance in glucose metabolism, PCK1 has become a potential drug target. Some research is exploring the possibility of regulating PCK1 activity to treat diseases related to blood sugar regulation.

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Specifications


Cat.No ACP04294 Target NamePCK1
Target Synonymscytosolic [GTP]; Phosphoenolpyruvate carboxykinase, cytosolic; Phosphoenolpyruvate carboxylase; Phosphopyruvate carboxylaseFormLiquid or Lyophilized powder
Expression SystemE.coliExpression Range1-622aa
Mol Weight73.2kDaProtein LengthFull length
PurityGreater than 90% as determined by SDS-PAGE.Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDP35558
Background Information
  • Uniprot Id

    P35558

  • Target Species

    Human

  • Target Name

    PCK1

  • Target Full Name

    Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

  • Target Function

    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.

  • Target Involvement

    Phosphoenolpyruvate carboxykinase deficiency, cytosolic (PCKDC)

  • Target Subcellular Location

    Cytoplasm, cytosol. Endoplasmic reticulum.

  • Target Protein Families

    Phosphoenolpyruvate carboxykinase [GTP] family

  • Target Tissue Specificity

    Major sites of expression are liver, kidney and adipocytes.

  • Target Research Area

    Metabolism

  • Target Synonyms

    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

  • Target Background

    This gene is a main control point for the regulation of gluconeogenesis. The cytosolic enzyme encoded by this gene, along with GTP, catalyzes the formation of phosphoenolpyruvate from oxaloacetate, with the release of carbon dioxide and GDP. The expression of this gene can be regulated by insulin, glucocorticoids, glucagon, cAMP, and diet. Defects in this gene are a cause of cytosolic phosphoenolpyruvate carboxykinase deficiency. A mitochondrial isozyme of the encoded protein also has been characterized.

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