Like ubiquitylation, phosphorylation is a reversible post-translational modification: Phosphorylation reactions involve the transfer of a phosphate group from a high-energy donor molecule, such as ATP, to a substrate protein or lipid, catalysed by enzymes called kinases and is a process central to intracellular signalling.
Abnormal protein phosphorylation is a cause or consequence of disease, including cancers, diabetes and inflammatory disease, while defects in genes that encode protein kinases and phosphatases underlie a number of inherited disorders. Around 500 protein kinases are encoded in the human genome and they account for around 25% of the molecular targets currently being pursued by drug discovery companies. It is becoming increasingly apparent that there is significant cross-talk between these two key intracellular systems; phosphorylation and ubiquitylation. For example TBK1 is an IKK-related kinase, which plays several important roles in the innate immune system. In the MyD88-dependent signaling pathway its activation requires the E3 ubiquitin ligase TRAF6 and the polyubiquitin-binding protein NEMO. TBK1 also plays an essential role in the production of type1 interferons that are produced in response to viral double-stranded RNA. This is triggered by the TBK1-catalysed activation of the transcription factor IRF3 and the E3 ubiquitin ligase Pellino 1.
|AMPKA1/AMPKB2/AMPKG1 [6His-tagged]||66-0041-050||50 µg||£250||View|
|AMPKA2/AMPKB2/AMPKG1 [6His-tagged]||66-0042-050||50 µg||£250||View|
|AMPK alpha 1 (T172D) [GST-tagged]||66-0040-050||50 µg||£250||View|
|B-Raf (V600E) [GST-tagged]||66-0023-050||50 µg||£325||View|
|B-Raf [GST-tagged]||66-0022-050||50 µg||£325||View|
|BRSK2 residues (2-674) [6His-tagged]||66-0001-050||50 µg||£250||View|
|C-Raf [GST-tagged]||66-0024-050||50 µg||£325||View|
|CHK2 [GST-tagged]||66-0019-050||50 µg||£325||View|
|IKK epsilon [GST-tagged]||66-0038-050||50 µg||£325||View|
|MAPK3 [untagged]||66-0026-050||50 µg||£325||View|