Recombinant Human DLL4 Fc Chimera Protein, CF Summary
| Additional Information |
Analyzed by SEC-MALS |
| Details of Functionality |
Measured by its binding ability in a functional ELISA. Recombinant Human DLL4 Fc Chimera (Catalog
# BT-DLL4) binds to Recombinant Human Notch-1 Fc Chimera (Catalog #
3647-TK) with
an ED 50 of 2.00-20.0 ng/mL. |
| Source |
Chinese Hamster Ovary cell line, CHO-derived human DLL4 protein Human DLL4 (Ser27-Pro524) Accession # Q9NR61.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | | N-terminus | | C-terminus | |
|
| N-terminal Sequence |
Ser 27 |
| Structure / Form |
Disulfide-linked homodimer |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>95%, by SDS-PAGE with 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 |
81 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 |
89-98 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 HBS and Tween®-80 with Trehalose. |
| Purity |
>95%, by SDS-PAGE with quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute the 20 μg size at 100 μg/mL
in water. Reconstitute all other sizes at 500 μg/mL in water. |
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 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). The use of DLL4, in conjunction with VCAM1, has been shown as an effective method for generating hematopoietic progenitors and T cells from hPSCs in a serum- and feeder-free environment.
- 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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