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 ED 50 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 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-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 |
|
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
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.
- 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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