Recombinant Human DLL1 Fc Chimera Protein, CF Summary
|Human DLL1 |
Accession # O00548
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 HEPES and EDTA.|
|Reconstitution||Reconstitute at 250 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.
Recombinant Human DLL1 Fc Chimera (Catalog # 10184-DL) enhances Recombinant Human BMP-2 (Catalog # 355-BM) induced alkaline phosphatase activity in the C3H10T1/2 mouse embryonic fibroblast cell line. The ED50for this effect is 0.1-0.5 µg/mL.
2 μg/lane of Recombinant Human DLL1 Fc Chimera was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 88-98 kDa and 170-190 kDa, respectively.
Delta-like protein 1 (DLL1) is a 90-100 kDa type I transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. Mature human DLL1 consists of a 528 amino acid (aa) extracellular domain (ECD) with one DSL domain and eight EGF-like repeats, a 23 aa transmembrane segment, and a 155 aa cytoplasmic domain (1). Within the ECD, human DLL1 shares 91% aa sequence identity with mouse and rat DLL1. It shares 26%, 37%, and 54% aa sequence identity with DLL2, 3, and 4, respectively. A 60 kDa ECD fragment released by ADAM9, 12, or 17 mediated proteolysis, promotes the proliferation of hematopoietic progenitor cells (2, 3). The residual membrane-bound portion of DLL1 can be cleaved by presenilin-dependent gamma -secretase, enabling the cytoplasmic domain to migrate to the nucleus (4). DLL1 localizes to adherent junctions on neuronal processes through its association with the scaffolding protein MAGI1 (5). DLL1 is widely expressed, and it plays an important role in embryonic somite formation, cochlear hair cell differentiation, plus B and T lymphocyte differentiation (6-11). The up-regulation of DLL1 in arterial endothelial cells following injury or angiogenic stimulation is central to postnatal arteriogenesis (12). DLL1 is also over-expressed in cervical carcinoma and glioma and contributes to tumor progression (1, 13). Soluble DLL-1 was shown to inhibit differentiation of hematopoietic precursor cells (14).
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