Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo.
Product Specifications | |
Application | IHC, ELISA |
Reactivity | Human |
Clonality | Monoclonal (Clone No.: 8F2) |
Documents & Links for Anti METAP2 mAb (Clone 8F2) | |
Datasheet | Anti METAP2 mAb (Clone 8F2) Datasheet |
Vendor Page | Anti METAP2 mAb (Clone 8F2) at CUSABIO |
Documents & Links for Anti METAP2 mAb (Clone 8F2) | |
Datasheet | Anti METAP2 mAb (Clone 8F2) Datasheet |
Vendor Page | Anti METAP2 mAb (Clone 8F2) |