Recombinant Human DLL3 Protein, CF Summary
Accession # Q9NYJ7-1
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 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.
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.
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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