| Bioactivity | Photo-lysine hydrochloride, a new lysine-based photo-reactive amino acid, captures proteins that bind lysine post-translational modifications. |
| Invitro | Photo-lysine is designed and synthesized by incorporating a photo-cross-linker (diazirine) into the side chain of natural lysine. Photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine post-translational modifications (PTMs), including ‘readers’ and ‘erasers’ of histone modifications. Photo-lysine can be incorporated into MDH2 and mediate photo-cross-linking to fix protein-protein interactions in cells. UV irradiation of cells in the presence of photo-lysine induced robust cross-linking of HSP90β and HSP60. Photo-lysine has higher efficiency than photo-leucine for photo-cross-linking of the two chaperone proteins. Photo-lysine enables capture of the heterodimer of proteins Ku70 and Ku80 within a protein complex. Photo-lysine enables identification of histone- and chromatin-binding proteins[1]. |
| Name | Photo-lysine hydrochloride |
| Formula | C6H14Cl2N4O2 |
| Molar Mass | 245.11 |
| Appearance | Solid |
| Transport | Room temperature in continental US; may vary elsewhere. |
| Storage | 4°C, protect from light, stored under nitrogen *In solvent : -80°C, 6 months; -20°C, 1 month (protect from light, stored under nitrogen) |
| Reference | [1]. Yang T, et al. Photo-lysine captures proteins that bind lysine post-translational modifications. Nat Chem Biol. 2016 Feb;12(2):70-2. |
Photo-lysine hydrochloride
CAS: F: C6H14Cl2N4O2 W: 245.11
Photo-lysine hydrochloride, a new lysine-based photo-reactive amino acid, captures proteins that bind lysine post-transl
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