• Purity

  >90%, by SDS-PAGE with silver staining.

• 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 Recombinant Human Neogenin is immobilized at 1.5 μg/mL (100 μL/well), the concentration of Recombinant Mouse Netrin?1 (Catalog # ) that produces 50% of the optimal binding response is approximately 15-75 ng/mL.

• Source

  Human embryonic kidney cell, HEK293-derived Ala34-Met1104, with a C-terminal 6-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Ala34

• Predicted Molecular Mass

  118 kDa

• SDS-PAGE

  130-153 kDa, reducing conditions

Background: Neogenin

Neogenin is a type I transmembrane protein belonging to the Ig superfamily. It is composed of an extracellular segment containing four Ig-like C2-type domains and six Fibronectin type III domains (1). Neogenin has a molecular weight of approximately 190 kDa, and the extracellular domain of the human protein shares 91% and 93% amino acid sequence identity with the mouse and rat orthologs, respectively (1). Four different isoforms are produced from alternative splicing of human   NEO1. Neogenin is widely expressed in adult human tissues with the highest levels being observed in skeletal muscle and pancreas (1). It is also ubiquitously expressed in both neuronal and non-neuronal tissues of the developing mouse embryo (2). Neogenin is a multifunctional cell-surface receptor that binds to members of the Netrin, Repulsive Guidance Molecule (RGM) and Bone Morphogenetic Protein (BMP) families (3-5). It has also been shown to interact with members of the UNC5 family and in certain instances, associate with CDO as a co-receptor (6-8). Neogenin appears to be involved in the regulation of multiple developmental processes including development of the central nervous system (CNS), myogenesis, angiogenesis, and formation of mammary glands (4, 5, 7-9). During CNS development, Neogenin regulates neural tube closure, neuronal differentiation, and cell survival (4, 5, 7). It also mediates Netrin-1-dependent attraction and RGM-A-dependent repulsion of growing axons (4, 5, 7, 10). Additionally, Neogenin binding to RGM and Netrin proteins regulates cell-cell adhesion, cell migration, tissue organization, and adult neurogenesis (4, 7, 11). Neogenin is thought to be involved in tumorgenesis and cancer cell invasiveness in brain and gastric cancers (12-14).

• References:

1. Meyerhardt, J.A. et al. (1997) Oncogene 14:1129.

2. Keeling, S.L. et al. (1997) Oncogene 15:691.

3. Hagihara, M. et al. (2011) J. Biol. Chem. 286:5157.

4. Tian, C. and J. Liu (2013) Mol. Reprod. Dev. 80:700.

5. Severyn, C.J. et al. (2009) Biochem. J. 422:393.

6. van den Heuvel, D.M. et al. (2013) PLoS ONE 8:e55828.

7. De Vries, M. and H.M. Cooper (2008) J. Neurochem. 106:1483.

8. Krauss, R.S. et al. (2005) J. Cell Sci. 118:2355.

9. Srinivasan, K. et al. (2003) Dev. Cell 4:371.

10. de Castro, F. (2003) News Physiol. Sci. 18:130.

11. O’Leary, C.J. et al. (2015) Stem Cells 33:503.

12. Milla, L.A. et al. (2014) Int. J. Cancer 134:21.

13. Akino, T. et al. (2014) Cancer Res. 74:3716.

14. Kim, S.J. et al. (2014) Oncotarget 5:3386.

• Entrez Gene IDs:

  4756 (Human); 18007 (Mouse)

• Alternate Names:

  HsT17534; IGDCC2DKFZp547B146; Immunoglobulin superfamily DCC subclass member 2; NEO; NEO1; neogenin (chicken) homolog 1; neogenin 1; neogenin homolog 1; Neogenin; NGN; NGNDKFZp547A066