DLL4 Mouse

DLL4 is a membrane-bound protein that consists of an extracellular domain, a transmembrane domain, and an intracellular domain . The extracellular domain contains multiple epidermal growth factor (EGF)-like repeats, which are essential for binding to Notch receptors . The intracellular domain is involved in signal transduction following receptor binding .

In terms of expression, DLL4 is induced by vascular endothelial growth factor (VEGF) and functions as a downstream modulator of VEGF-mediated angiogenesis . It is primarily expressed in arterial endothelial cells and is upregulated in tumor vasculature .

DLL4/Notch signaling plays a pivotal role in vascular development by restraining excessive branching and sprouting of endothelial cells in response to VEGF signaling . This signaling pathway is essential for the proper formation of blood vessels and the maintenance of vascular integrity . Deletion of a single copy of DLL4 results in severe vascular defects and embryonic lethality, highlighting its critical role in vascular development .

In the context of cancer, DLL4 is upregulated in tumor vasculature, and the blockade of DLL4/Notch signaling has been shown to inhibit tumor growth by increasing functionally defective vasculature . This makes DLL4 a potential target for anti-angiogenic therapies in cancer treatment .

Recombinant Mouse DLL4 is produced using various expression systems, including mouse myeloma cell lines and 293E cells . The recombinant protein is typically tagged with a His-tag for purification purposes and is available in both carrier-free and carrier-containing formulations . The carrier protein, often bovine serum albumin (BSA), enhances protein stability and shelf-life .

The recombinant protein is used in various research applications, including studies on angiogenesis, cancer, and vascular development . It is also utilized in assays to measure its ability to enhance BMP-2 or BMP-9 induced alkaline phosphatase activity in mouse embryonic fibroblast cells .