For immunochemical detection of PEPCK
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PEPCK Polyclonal Antibody

Item No. 10004943

Technical Information
Synonyms
  • Pck1
  • PEPCK-c
  • Phosphoenolpyruvate carboxykinase
Immunogen
Peptide from the N-terminal region of mouse PEPCK
500 µl of peptide affinity-purified polyclonal antibody
Storage Buffer
PBS, pH 7.2, with 50% glycerol and 0.02% sodium azide
Host
Rabbit
Applications
WB
Species Reactivity
(+) Mouse PEPCK(+) Rat PEPCK
UniProt Accession №
Q9Z2V4
Origin
Animal/Rabbit
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Phosphoenolpyruvate carboxykinase (PEPCK) is a hormonally regulated enzyme responsible for the first committed step in gluconeogenesis, catalyzing the conversion of oxaloacetate to phosphoenolpyruvate.1,2 PEPCK mRNA is most abundant in the liver, kidney cortex, and white adipose tissue but is also found in brown fat, the mammary gland during lactation, and the small intestine.2 Both non-insulin-dependent diabetes mellitus and streptozotocin-induced diabetes result in elevated PEPCK activity, protein, and mRNA.1,3 Two isozymes of PEPCK have been identified, cytosolic and mitochondrial.4 Cayman’s PEPCK polyclonal antibody was generated against murine cytosolic PEPCK and detects the protein at 68 kDa by western blotting in rat and murine samples.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Friedman, J.E., Yun, J.S., Patel, Y.M., et alGlucocorticoids regulate the induction of phosphoenolpyruvate carboxykinase (GTP) gene transcription during diabetes. The Journal of Biological Chemisty 268(17), 12952-12957 (1993).

    2. Rajas, F., Croset, M., Zitoun, C., et alInduction of PEPCK gene expression in insulinopenia in rat small intestine. Diabetes 49, 1165-1168 (2000).

    3. Veneziale, C.M., Donofrio, J.C., and Nishimura, H. The concentration of P-enolpyruvate carboxykinase protein in murine tissues in diabetes of chemical and genetic origin. The Journal of Biological Chemisty 258(23), 14257-14262 (1983).

    4. Weldon, S.L., Rando, A., Matathias, A.S., et alMitochondrial phosphoenolpyruvate carboxykinase from the chicken. Comparison of the cDNA and protein sequences with the cytosolic isozyme. The Journal of Biological Chemisty 265(13), 7308-7317 (1990).

    Product Citations

    Knudsen, J.G., Gudiksen, A., Bertholdt, L., et alSkeletal muscle IL-6 regulates muscle substrate utilization and adipose tissue metabolism during recovery from an acute bout of exercise. PLoS One 12(12), e0189301 (2017).

    Knudsen, J.G., Bertholdt, L., Joensen, E., et alSkeletal muscle interleukin-6 regulates metabolic factors in iWAT during HFD and exercise training. Obesity (Silver Spring) 23(8), 1616-1624 (2015).

    Buzelle, S.L., MacPherson, R.E.K., Peppler, W.T., et alThe contribution of IL-6 to beta 3 adrenergic receptor mediated adipose tissue remodeling. Physiol. Rep. 3(2), e12312 (2015).

    Wan, Z., Ritchie, I., Beaudoin, M.-S., et alIL-6 indirectly modulates the induction of glyceroneogenic enzymes in adipose tissue during exercise. PLoS One 7(7), e41719 (2012).