Recombinant Porcine DLL4 Fc Chimera Protein, CF Summary
Accession # NP_001231347.1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Recombinant Porcine DLL4 Fc Chimera Protein (10508-DL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 89-99 kDa and 160-190 kDa, respectively.
Delta-like protein 4 (DLL4) is a type I membrane protein belonging to the Delta/Serrate/Lag2 (DSL) family of Notch ligands (1). Notch signaling is an evolutionarily conserved pathway that controls cell fate and is required in multiple developmental processes including vascular development, hematopoiesis, somatogenesis, myogenesis, and neurogenesis (2 - 4). Dysregulation in the Notch pathway is associated with various human diseases. In mammals, four Notch homologs (Notch 1 to 4) and five ligands (DLL 1, 3 and 4, Jagged 1 and 2) have been identified. Notch ligands are transmembrane proteins with a DSL motif necessary for Notch binding, tandem EGF repeats, a transmembrane region and a short intracellular domain (ICD). Porcine DLL4 cDNA encodes a 685 amino acid (aa) residue precursor protein that shares 92% aa sequence homology with human DLL4 in the extracellular domain. Notch ligands are categorized into two subfamilies based on the presence of an extracellular cysteine-rich domain and insertions that interrupt some EGF repeats in the Jagged but not the Delta ligand family. Interactions of Notch receptors with their ligands results in reciprocal regulated intramembrane proteolysis (RIP) (4). RIP is a mechanism for transmembrane signal transduction that involves the sequential processing by a disintegrin metalloprotease (ADAM) and then by presenilin/ gamma secretase, resulting in shedding of the extracellular domains and the generation of the soluble ICD signaling fragments, respectively. The Notch ICD translocates to the nucleus and interacts with transcriptional coactivators, resulting in the transcription of target genes. The ICDs of the Notch ligands have also been shown to translocate to the nucleus where they may have a signaling function (5, 6). DLL4 is expressed highly and selectively within the arterial endothelium and has been shown to function as a ligand for Notch 1 and Notch 4. Human and mouse DLL4 share 86% amino acid sequence identity (1).
- Shutter, J.R. et al. (2000) Genes Dev. 14:1313.
- Iso, Tatsuya et al. (2002) Arterioscler. Thromb. Vasc. Biol. 23:543.
- Walker, L. et al. (2001) Stem Cells 19:543.
- Baron, M. (2002) Semin. Cell Dev. Biol. 14:113.
- Ikeuchi, T. and S.S. Sisodia (2003) J. Biol. Chem. 278:7751.
- Bland, C.E. et al. (2003) J. Biol. Chem. 278:13607.
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