2 μg/lane of Recombinant Human DLL3 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® blue staining, showing bands at 52-62 kDa and 40-55 kDa, respectively.
>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
Theoretical MW
49 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
52-62 kDa, reducing conditions
Publications
Read Publications using 9749-DL in the following applications:
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.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 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 DLL3 Protein, CF
delta (Drosophila)-like 3
Delta3
delta-like 3 (Drosophila)
delta-like protein 3
DLL3
Drosophila Delta homolog 3
Pudgy
SCDO1
SCDO1delta3
Background
Delta-like
protein 3 (DLL3) is a transmembrane protein that belongs to the
Delta/Serrate/Lag-2 (DSL) family of Notch ligands (1). Mature human DLL3
consists of a 466 amino acid (aa) extracellular domain (ECD) with one DSL
domain and six EGF-like repeats, a 21 aa transmembrane segment, and a 105 aa cytoplasmic domain (2). Within the ECD, human DLL3 shares 86% aa
sequence identity with mouse and rat DLL3. DLL3
is known as a divergent DSL ligand since it does not function in similar manner
as the rest of DSL ligands. It does not activate Notch signaling through
trans-activation, but autonomously attenuates signaling induced by other DSL ligands
(3). A loss-of-function mutation of
DLL3 is linked to axial skeletal defects in the spondylocostal dysplasia,
which is linked to abnormal Notch signaling (4). DL-3 promotes proliferation and inhibits
apoptosis of cancer cells. The proliferative effect mediated by DLL3 is
thought to be due to increased Akt phosphorylation in cancer cells (5).
Dunwoodie, S. L. et al. (1997) Development 124:3065.
Bulman, M. P. et al. (2000) Nat. Genet. 24:438.
Ladi, E. et al. (2005) J. Cell Biol. 170:983.
Dunwoodie, S.L. et al. (2002) Development 129:1795.
Deng S.M. et al. (2017) Biochem. Biophys. Res. Commun. 483:488.
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