Recombinant Human Semaphorin 3E Protein, CF

Product Discontinued

Recombinant Human Semaphorin 3E Protein, CF Summary

• Details of Functionality: 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 ED₅₀ for this effect is 0.3-1.5 μg/mL. Measured by its binding ability in a functional ELISA. When Recombinant Human Plexin D1 (Catalog # 4160-PD) is coated at 5 μg/mL, Recombinant Human Semaphorin 3E binds with an apparent K_D <2 nM.
• Source: Mouse myeloma cell line, NS0-derived human Semaphorin 3E protein
  Thr25-Ser775 (Arg557Ala and Arg560Ala), with an N-terminal 10-His tag
• Accession #: O15041
• N-terminal Sequence: His
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity2
  • Bioactivity
• Theoretical MW: 87.9 kDa (monomer).
  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: 90 kDa, 66 kDa and 25 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 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS and Tween® 20.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Semaphorin 3E Protein, CF

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

Background

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).

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.

Publications for Semaphorin 3E (3239-S3)(5)

Publications using 3239-S3

• MT Haider, H Saito, J Zarrer, K Uzhunnumpu, S Nagarajan, V Kari, M Horn-Gland, S Werner, E Hesse, H Taipaleenm Breast cancer bone metastases are attenuated in a Tgif1-deficient bone microenvironment Breast Cancer Res., 2020-04-09;22(1):34. 2020-04-09 [PMID: 32272947] (Migration Bioassay, Human)
• Coronary vasculature patterning requires a novel endothelial ErbB2 holoreceptor Nat Commun, 2016-06-30;7(0):12038. 2016-06-30 [PMID: 27356767] (Bioassay, Human)
• Kusuhara , Sentaro, Fukushima , Yoko, Fukuhara , Shigetom, Jakt , Lars Mar, Okada , Mitsuhir, Shimizu , Yuri, Hata , Masayuki, Nishida , Kohji, Negi , Akira, Hirashima , Masanori, Mochizuki , Naoki, Nishikawa , Shin-Ich, Uemura , Akiyoshi Arhgef15 promotes retinal angiogenesis by mediating VEGF-induced Cdc42 activation and potentiating RhoJ inactivation in endothelial cells. PLoS ONE, 2012-09-21;7(9):e45858. 2012-09-21 [PMID: 23029280] (Bioassay, Human)
• Meda C, Molla F, De Pizzol M Semaphorin 4A exerts a proangiogenic effect by enhancing vascular endothelial growth factor-A expression in macrophages. J. Immunol., 2012-03-21;188(8):4081-92. 2012-03-21 [PMID: 22442441] (Bioassay, Human)
• Fukushima Y, Okada M, Kataoka H Sema3E-PlexinD1 signaling selectively suppresses disoriented angiogenesis in ischemic retinopathy in mice. J. Clin. Invest., 2011-04-18;121(5):1974-85. 2011-04-18 [PMID: 21505259] (Bioassay, In Vivo, Human, Mouse)

Bioinformatics

• Uniprot:
  • O15041()