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Recombinant Mouse DLL1 His-tag Protein, CF

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Immobilized Recombinant Mouse DLL1 His-tag Protein (10507-DL) enhances Recombinant Human BMP-2 (355-BM) induced alkaline phosphatase activity in C3H10T1/2 mouse embryonic fibroblast cells. The ED50 for this effect is ...read more
2 μg/lane of Recombinant Mouse DLL1 His-tag Protein (10507-DL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 58-67 kDa ...read more

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse DLL1 His-tag Protein, CF Summary

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. et al. (2005) J. Biol. Chem. 280:15842. The ED50 for this effect is 0.8-4 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse DLL1 protein
Ser22- Gln516, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser22
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
55 kDa.
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
58-67 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 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 Mouse DLL1 His-tag 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 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).

  1. Bettenhausen, B. et al. (1995) Development 121:2407.
  2. Dyczynska, E. et al. (2007) J. Biol. Chem. 282:436.
  3. Karanu, F.N. et al. (2001) Blood 97:1960.
  4. Ikeuchi, T. and S.S. Sisodia (2003) J. Biol. Chem. 278:7751.
  5. Mizuhara, E. et al. (2005) J. Biol. Chem. 280:26499.
  6. Takahashi, Y. et al. (2003) Development 130:4259.
  7. Teppner, I. et al. (2007) BMC Dev. Biol. 7:68.
  8. Kiernan, A.E. et al. (2005) Development 132:4353.
  9. Schmitt, T.M. and J.C. Zuniga-Pflucker (2002) Immunity 17:749.
  10. Hozumi, K. et al. (2004) Nat. Immunol. 5:638.
  11. Shimojo, H. et al. (2008) Neuron 58:52.
  12. Schuster-Gossler, K. et al. (2007) Proc. Natl. Acad. Sci. 104:537.
  13. Limbourg, A. et al. (2007) Circ. Res. 100:363.
  14. Purow, B.W. et al. (2005) Cancer Res. 65:2353.
  15. Gray, G.E. et al. (1999) Am. J. Pathol. 154:785.

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