Human sDLL-4 comprises the extracellular signaling domain of DLL, a member of a structurally-related family of single-pass type I trans-membrane proteins that serve as ligands for Notch receptors. DLL-4 functions to specifically activate the Notch-1 and Notch-4 receptors. The Notch signaling pathway regulates endothelial cell differentiation, proliferation and apoptosis, and is essential for the development, maintenance and remodeling of the vascular system. Targeted deletion of the DLL-4 gene in mice resulted in severe vascular defects and death before birth. Up-regulation of DLL-4 expression has been implicated in the vascular development of certain tumors. The human DLL-4 gene consists of a 503 amino acid extracellular domain with one DSL domain, eight EGF-like repeats, a 21 a.a. transmembrane domain, and a 135 a.a. cytoplasmic domain. Recombinant Human sDLL-4 is a 54.3 kDa glycoprotein containing 498 amino acid residues.
Amino Acid Sequence
The sDLL-4, when immobilized at concentrations > 1.5 µg/mL will inhibit myogenesis in C2C12 cells.
Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.