|Application ||WB, E|
|Calculated MW||54122 Da|
|Other Names||Pyruvate dehydrogenase protein X component, mitochondrial, Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex, E3-binding protein, E3BP, Lipoyl-containing pyruvate dehydrogenase complex component X, proX, PDHX, PDX1|
|Target/Specificity||This PDX1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 429-459 amino acids from the C-terminal region of human PDX1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PDX1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.|
|Cellular Location||Mitochondrion matrix.|
Provided below are standard protocols that you may find useful for product applications.
PDX1, located in the mitochondrial matrix, is required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by noncovalent bonds. Defects in PDHX are a cause of lacticacidemia. PDX1 belongs to the 2-oxoacid dehydrogenase family and contains 1 lipoyl-binding domain.
Ling, M., et al., Hum. Mol. Genet. 7(3):501-505 (1998). Harris, R.A., et al., J. Biol. Chem. 272(32):19746-19751 (1997). Murray, J., et al., FEBS Lett. 529 (2-3), 173-178 (2002).