Recombinant Rat DLL1 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA.<br />When rrNotch-1 (Catalog # 1057-TK) is coated at 5 μg/mL, rrDLL-1 binds with an apparent K<SUB>D </SUB><5 nM.<br /><br />
<0.100 EU per 1 µg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
82.6 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
90-95 kDa, reducing conditions
Publications
Read Publication using 3970-DL in the following applications:
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 PBS.
Reconstitution Instructions
Reconstitute at 200 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 Rat DLL1 Fc Chimera Protein, CF
delta (Drosophila)-like 1
Delta 1
Delta
Delta1
delta-like 1 (Drosophila)
delta-like protein 1
DL1
DLL1
Drosophila Delta homolog 1
H-Delta-1
Background
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 rat DLL1 consists of a 520 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, rat DLL1 shares 90% and 95% aa sequence identity with human and mouse DLL1, respectively. It shares 26%, 36%, and 53% aa sequence identity with rat DLL2, 3, and 4, respectively. The ADAM9, 12, or 17‑ mediated proteolysis of DLL1 releases a 60 kDa ECD fragment and regulates the Notch-dependent proliferation of hematopoietic and myogenic progenitor cells (2 ‑ 4). The residual membrane-bound portion of DLL1 can be cleaved by presenilin-dependent gamma -secretase, enabling the cytoplasmic domain to migrate to the nucleus (5). DLL1 localizes to adherens junctions on neuronal processes through its association with the scaffolding protein MAGI1 (6). 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 (4, 7 ‑ 13). The up‑regulation of DLL1 in arterial endothelial cells following injury or angiogenic stimulation is central to postnatal arteriogenesis (14). DLL1 is also overexpressed in cervical carcinoma and glioma and contributes to tumor progression (15 ‑ 16).
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Ikeuchi, T. and S.S. Sisodia (2003) J. Biol. Chem. 278:7751.
Mizuhara, E. et al. (2005) J. Biol. Chem. 280:26499.
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Teppner, I. et al. (2007) BMC Dev. Biol. 7:68.
Kiernan, A.E. et al. (2005) Development 132:4353.
Schmitt, T.M. and J.C. Zuniga-Pflucker (2002) Immunity 17:749.
Hozumi, K. et al. (2004) Nat. Immunol. 5:638.
Shimojo, H. et al. (2008) Neuron 58:52.
Schuster-Gossler, K. et al. (2007) Proc. Natl. Acad. Sci. 104:537.
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