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Protein Tag: N-His
Uniprot: P07379
Accession: P07379
Background: PCK1 (Phosphoenolpyruvate carboxykinase 1, also PEPCK-C [cytosolic]) is a monomeric, 67-68 kDa member of the PEP carboxykinase family of enzymes. It is expressed in postnatal cells such as mammary epithelium, white and brown adipocytes, skeletal muscle cells and hepatocytes. PCK1 has multiple functions, some of which are cell-specific. In particular, PCK1 has both cataplerotic (Greek: to fill down, or remove) and anaplerotic (to fill up, or replace) activity, where it removes and replaces elements of the TCA cycle. It is also gluconeogenic, and promotes glucose formation via PEP generation. Finally, it is glyceroneogenic, creating glycerol-3-phosphate that is used to reesterify and store just-released free fatty acids in adipocytes. It contains one kinase domain (aa 27-615), and two potential acetylation sites at Lys70 and 71. There are four potential splice forms. Two have alternative start sites at Met460 and Met315, while two others show a deletion of aa 34-546, plus a three aa substitution for aa 85-204, respectively.
Bio Acitivity: Not validated for activity
Sequence: Met 1-Lys 135
Purity: > 95% as determined by reducing SDS-PAGE.
Formulation: Lyophilized from sterile PBS, pH 7.4.
Normally 5%-8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.
Endotoxin: < 10 EU/mg of the protein as determined by the LAL method.
Calculated MW: 14.7 kDa
Observed MW: 15 kDa
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