Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. When rrNotch-1 (Catalog # 1057-TK) is coated at 5 μg/mL, rrDLL-1 binds with an apparent K D <5 nM.
Source
Chinese Hamster Ovary cell line, CHO-derived
Rat DLL-1
(Ser22 - Ser534)
Accession # P97677IEGRMDP Mouse IgG2A
(Glu98 - Lys330)N-terminus C-terminus Accession #
N-terminal Sequence
AnalysisSer22
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
82.6 kDa (monomer)
SDS-PAGE
90-95 kDa, reducing conditions
3970-DL |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
Reconstitution Reconstitute at 200 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.
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Background: DLL1
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).
References:
Bettenhausen, B. et al. (1995) Development 121:2407.
Dyczynska, E. et al. (2007) J. Biol. Chem. 282:436.
Karanu, F.N. et al. (2001) Blood 97:1960.
Sun, D. et al. (2008) J. Cell Sci. 121:3815.
Ikeuchi, T. and S.S. Sisodia (2003) J. Biol. Chem. 278:7751.
Mizuhara, E. et al. (2005) J. Biol. Chem. 280:26499.
Takahashi, Y. et al. (2003) Development 130:4259.
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.
Limbourg, A. et al. (2007) Circ. Res. 100:363.
Purow, B.W. et al. (2005) Cancer Res. 65:2353.
Gray, G.E. et al. (1999) Am. J. Pathol. 154:785.
Long Name:
Delta-like 1
Entrez Gene IDs:
28514 (Human); 13388 (Mouse); 84010 (Rat)
Alternate Names:
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
