Novel HIF2A mutations disrupt oxygen sensing, leading to polycythemia, paragangliomas, and somatostatinomas Blood, Mar 2013; 121: 2563 - 2566.
[anti-HA]
Regulation of the PI3-K/Akt Survival Pathway in the Rat Endometrium Biol Reprod, Mar 2013; 88: 79.
[Akt3]
RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP Nucleic Acids Res., Mar 2013; 10.1093/nar/gkt159.
[LA]
Ruxolitinib as potential targeted therapy for patients with JAK2 rearrangements Haematologica, Mar 2013; 98: 404 - 408.
[JAK2]
A synthetic peptide corresponding to residues surrounding serine 221 of human ACC2 was used as an immunogen.
Buffer
Store at -20C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
Acetyl-CoA carboxylase 2 (ACC2) is a biotin-dependent enzyme that is involved in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. ACC2 is predominantly expressed in the heart, skeletal muscles and liver (1). It catalyzes the irreversible carboxylation of acetyl-CoA to produce malonyl-CoA through its two catalytic activities, biotin carboxylase and carboxyltransferase. ACC2 is throught to control fatty acid oxidation by the means of the ability of malonyl-CoA to inhibit carnitine-palmitoyl-CoA transferase I (CPT-1), the rate-limiting step in fatty acid uptake and oxidation by mitochondria (2). The activity of ACC2 is controlled by reversible phosphorylation. Ser219 and Ser221 were found to be critical for the phosphorylation and subsequent inactivation of ACC2 (3).
Related Pathway
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