| Reactivity | MuSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Details of Functionality | Measured by the ability of the immobilized protein to enhance BMP-2 induced alkaline phosphatase activity in C3H10T1/2 mouse embryonic fibroblast cells. Nobta, M. <EM>et al</EM>. (2005) J. Biol. Chem. <STRONG>280</STRONG>:15842.<br />The ED<sub>50</sub> for this effect is 0.25-1 μg/mL. <br /><br /> |
| Accession # | |
| N-terminal Sequence | Ser22 |
| Structure / Form | Disulfide-linked homodimer |
| Protein/Peptide Type | Recombinant Proteins |
| Gene | Dll1 |
| Endotoxin Note | <0.100 EU per 1 µg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 81.4 kDa (monomer). 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 kDa, reducing conditions |
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| Publications |
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| Storage | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
| Buffer | Lyophilized from a 0.2 μm filtered solution in HEPES and EDTA. |
| Reconstitution Instructions | Reconstitute at 500 μg/mL in sterile PBS. |
Delta-like protein 1 (DLL1) is a 90-100 kDa type I transmembrane protein in the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. Mature mouse 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 154 aa cytoplasmic domain (1). Within the ECD, mouse DLL1 shares 91% and 95% aa sequence identity with human and rat DLL1, respectively. It shares 26%, 35%, and 51% 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 adherens 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, lymphocyte differentiation, and the maintenance of neural and myogenic progenitor cells (6-12). The up-regulation of DLL1 in arterial endothelial cells following injury or angiogenic stimulation is central to postnatal arteriogenesis (13). DLL1 is also over-expressed in cervical carcinoma and glioma and contributes to tumor progression (14, 15).
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