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Recombinant Human DLL4 Fc Chimera Avi-tag Protein, CF

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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 ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human DLL4 Fc Chimera Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Notch-1 Fc Chimera (Catalog # 3647-TK) is coated at 250 ng/mL (100 μL/wll), Biotinylated Recombinant Human DLL4 Fc Chimera Avi-tag protein binds with an ED50 of 0.012-0.12 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human DLL4 protein
Human DLL4
(Ser27-Pro524)
Accession # Q9NR61.1
IEGRMDHuman IgG1
(Pro100-Lys330)
Avi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Ser27
Structure / Form
Disulfide-linked homodimer, biotinylated via Avi-tag
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
83 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
94-112 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human DLL4 Fc Chimera Avi-tag Protein, CF

  • Delta 4 precursor
  • delta 4
  • delta ligand 4
  • delta4
  • delta-like 4 (Drosophila)
  • delta-like 4 homolog (Drosophila)
  • delta-like 4 homolog
  • delta-like 4 protein
  • delta-like protein 4
  • DLL4
  • Drosophila Delta homolog 4
  • hdelta2
  • MGC126344
  • notch ligand delta-2
  • notch ligand DLL4

Background

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.
  1. Shutter, J.R. et al. (2000) Genes Dev. 14:1313.
  2. Iso, Tatsuya et al. (2002) Arterioscler. Thromb. Vasc. Biol. 23:543.
  3. Walker, L. et al. (2001) Stem Cells 19:543.
  4. Baron, M. (2002) Semin. Cell Dev. Biol. 14:113.
  5. Ikeuchi, T. and S.S. Sisodia (2003) J. Biol. Chem. 278:7751.
  6. Bland, C.E. et al. (2003) J. Biol. Chem. 278:13607.

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