Recombinant Human Notch-4 Fc Chimera Protein, CF

When Recombinant Human DLL4 (Catalog # 1506-D4) isimmobilized at 2 ug/mL, Recombinant Human Notch-4 Fc Chimera (Catalog #9909-NT) binds with an ED50 of 0.5‑2.5 μg/mL.

2μg/lane of Recombinant Human Notch‑4 was resolved with SDS-PAGEunder reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 94-116 kDa and 170-200 kDa,respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Notch-4 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human DLL4 (Catalog # 1506-D4) is immobilized at 2 μg/mL, 100 μL/well, the concentration of Recombinant Notch-4 Human Fc Chimera that produces 50% of the optimal binding response is 0.5-2.5 μg/mL.
• Source: Trichoplusia ni, T. ni (baculovirus)-derived human Notch-4 protein
  

  Human Notch‑4 (Arg24-Glu549) Accession # Q99466-1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q99466-1
• N-terminal Sequence: Arg24
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, 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: 82 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: 94-116 kDa, 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 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 400 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 Human Notch-4 Fc Chimera Protein, CF

• INT3
• neurogenic locus notch homolog protein 4
• notch 4
• Notch homolog 4
• NOTCH3
• Notch4
• Notch-4

Background

Human Notch-4 is a 300 kDa type I transmembrane glycoprotein that is one of four human Notch homologues involved in developmental processes (1-3). Human Notch-4 is synthesized as a 2003 amino acid (aa) precursor that contains a 23 aa signal sequence, a 1424 aa extracellular domain (ECD) with 29 EGF-like repeats and three Lin-12/Notch repeats (LNR), a 21 aa transmembrane (TM) segment and a 535 aa cytoplasmic domain containing five ankyrin repeats (1, 3). Within the expressed region of this product (including EGF domains 1-13) human Notch-4 shares 84%, 83%, 51%, and 48% aa sequence identity with mouse Notch-4, rat Notch-4, human Notch-2 and human Notch-1 respectively. The 11th and 12th EGF-like repeats bind ligands including Jagged and Delta-like families in humans (4). Delta-like ligand-4 (DLL4)-Notch-4 signaling correlates to angiogenesis in glioblastomas (5). Notch-4 has been identified as a key player in invasive cancers such as breast cancer, hepatocellular carcinoma, melanoma, and prostate cancer (6-9). Notch-4 expression in 3T3L preadipocytes enhanced their proliferation and adipogenesis though up‑regulation of adipogenic genes such as C/EBP alpha , PPAR gamma , aP2, LPL and HSL (10). It has also been shown to be involved in proliferation of gastric cancer though Wnt-1/ beta -catenin signaling regulation (11).

1. Dumortier, A. et al. (2005) Int. J. Hematol. 82:277.
2. Yoon, K. and N. Gaiano (2005) Nat. Neurosci. 8:709.
3. Leong, K.G. and A. Karsan (2006) Blood 107:2223.
4. Hambleton, S. et al. (2004) Structure 12:2173.
5. Zhang, J.F. et al. (2016) Tumour Biol. 37:3797.
6. Yao, K. et al. (2011) Int. J. Surg. Pathol. 19:607.
7. Gramantieri, L. et al. (2007) Liver Int. 27:997.
8. Lin, X. et al. (2016) Cancer Sci. 107:1079.
9. Zhang, J. et al. (2017) Apoptosis. 22:877.
10. Lai, P.Y. et al. (2013) Biochem. Biophys. Res. Commun. 430:1132.
11. Qian, C. et al. (2015) Mol. Cell. Biochem. 401:165.

Bioinformatics

• Uniprot:
  • Q99466-1()