Recombinant Human DLL1 (carrier-free)

DLL1 is a member of the Delta/Serrate/Lag2 (DSL) family of ligands that bind the Notch receptor. Five DSL ligands have been identified in mammals including three Delta-like proteins (Dll1, 3, and 4) and two Serrate-like (Jagged1 and Jagged2). The canonical DSL (Delta, Serrate, Lag2) ligands are type I cell surface proteins, and like Notch have tandem EGF repeats in their extracellular domain. The DSL domain, the amino terminal, and the first two EGF domains are necessary for the binding to the Notch receptor. Jagged1 and Jagged2 have an additional cysteine rich region, not present in the Delta-like proteins. Through a cell-cell interaction the Notch signaling is activated (trans-interaction); the interaction of the ligands with Notch within the same cell (cis-interaction) induces inhibitory cell signaling. The Notch signaling pathway plays important roles in specifying cell fate during embryonic development and contributes to adult homeostasis; thus, Notch plays a key role in the development of embryonic hematopoietic stem cells, modulates T cell-mediated immune responses and development of marginal zone (MZ) B cells. DLL1 enhances the in vitro conversion of human memory CD4 T cells into FOXP3-expressing regulatory T cells. DSL ligands are cleaved by ADAMs (ADAM9, 10, 12, and 17) resulting in the shedding of the extracellular domain. Soluble intracellular derivatives are generated by presenilin-dependent intramembranous gamma-secretase processing. DLL1 intracellular domain (DICD) generated by the gamma-cleavage is transported into the nucleus where it plays a role in transcriptional events.