Recombinant Human DLL4 Fc Chimera Avi-tag Protein, CF
Recombinant Human DLL4 Fc Chimera Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
Human DLL4 (Ser27-Pro524) Accession # Q9NR61.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag |
N-terminus | C-terminus | ||
Analysis
Product Datasheets
Carrier Free
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.
AVI10185
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 250 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.
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Scientific Data
When Recombinant Human Notch-1 Fc Chimera (3647-TK) is coated at 250 ng/mL (100 μL/well), Biotinylated Recombinant Human DLL4 Fc Chimera Avi-tag (Catalog # AVI10185) binds with an ED50 of 0.012-0.12 μg/mL.
2 μg/lane of Biotinylated Recombinant Human DLL4 Fc Chimera Avi-tag Protein (Catalog # AVI10185) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at kDa 94-112 and 180-210 kDa, respectively.
Reconstitution Calculator
Background: DLL4
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). 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). Our Avi-tag Biotinylated human DLL4 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- 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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