Recombinant Human Semaphorin 3E Protein, CF 25 UG

• Purity

  >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

• Endotoxin Level

  <1.0 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its ability to inhibit the proliferation of HUVEC human umbilical vein endothelial cells. Moriya, J.     et al. (2010) Circ. Res.     106:391. The ED    ₅₀ for this effect is 0.04-0.24 μg/mL. Measured by its binding ability in a functional ELISA. When Recombinant Human Plexin D1 (Catalog # ) is coated at 5 μg/mL, Recombinant Human Semaphorin 3E binds with an apparent K    _d <0.4 nM.    

  
  

• Source

  Mouse myeloma cell line, NS0-derived His24-Ser775 (Arg557Ala and Arg560Ala), with an N-terminal 10-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  His

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  88 kDa

• SDS-PAGE

  85-100 kDa, 66 kDa and 25 kDa, reducing conditions

Background: Semaphorin 3E

Semaphorin 3E (Sema3E), previously known as SemaH, is one of six Class 3 (secreted) semaphorins which function in axon guidance and/or vascular tip cell guidance during development (1). Sema3E contains a seven-blade beta -propeller sema domain, a cysteine-knot PSI domain, an Ig-like domain, and a basic region. Dimerization and cleavage within the basic region are required for the repulsing activity of class 3 semaphorins (2). Sema3E can also be cleaved at a furin consensus sequence C-terminal to the sema domain, resulting in a 61 kDa form that does not dimerize and is highly expressed in tumor cell lines with metastatic potential (3, 4). Mature human Sema3E shares 90% aa sequence identity with mouse and rat Sema3E. Alternative splicing generates a short isoform that lacks the signal peptide and the N-terminal 35 residues of the mature protein. Sema3E signaling is transduced by Plexin D1 which may also be associated with Neuropilin 1 and/or VEGF R2 (2, 5, 6). Its interaction with Plexin D1 inhibits axon migration in the neocortex and forebrain (6, 7), although it can attract axons that express both Plexin D1 and Neuropilin 1 (6). Sema3E promotes axonal growth (5), the development of glutamatergic synaptic specificity (8, 9), and the development of GnRH producing neurons (10). Genetic disruption of either Sema3E or Plexin D1 in mouse causes excessive and disorganized vascular growth and branching, indicating the importance of this ligand-receptor pair for vascular guidance (11, 12). In addition, Sema3E is up-regulated by inflammatory macrophages and damaged hepatocytes (13-15). It inhibits smooth muscle cell proliferation and migration in the asthmatic airway (16), promotes hepatic stellate cell activation and wound healing (15), and regulates the migration of developing thymocytes (17).

• References:

1. Oh, W.J. and C. Gu (2013) Semin. Cell Dev. Biol. 24:156.

2. Adams, R. H. et al. (1997) EMBO J. 16:6077.

3. Christensen, C. et al. (2005) Cancer Res. 65:6167.

4. Casazza, A. et al. (2010) J. Clin. Invest. 120:2684.

5. Bellon, A. et al. (2010) Neuron 66:205.

6. Chauvet, S. et al. (2007) Neuron 56:807.

7. Bribian, A. et al. (2014) Nat. Commun. 5:4265.

8. Ding, J.B. et al. (2011) Nat. Neurosci. 15:215.

9. Pecho-Vrieseling, E. et al. (2009) Nature 459:842.

10. Cariboni, A. et al. (2015) J. Clin. Invest. 125:2413.

11. Gu, C. et al. (2005) Science 307:265.

12. Gitler, A. D. et al. (2004) Developmental Cell 7:107.

13. Wanschel, A. et al. (2013) Arterioscler. Thromb. Vasc. Biol. 33:886.

14. Shimizu, I. et al. (2013) Cell Metab. 18:491.

15. Yagai, T. et al. (2014) Am. J. Pathol. 184:2250.

16. Movassagh, H. et al. (2014) J. Allergy Clin. Immunol. 133:560.

17. Choi, Y.I. et al. (2014) Proc. Natl. Acad. Sci. USA 111:379.

• Entrez Gene IDs:

  9723 (Human); 20349 (Mouse)

• Alternate Names:

  (semaphorin) 3E; coll-5; KIAA0331M-SEMAH; sema domain, immunoglobulin domain (Ig), short basic domain, secreted; Sema3E; SEMAH; SEMAHM-SemaK; Semaphorin 3E; semaphorin-3E