Recombinant Human Semaphorin 3F Fc Chimera Protein, CF

When Recombinant Human Neuropilin‑2 Fc Chimera (Catalog # 2215-N2) is immobilized at 2 μg/mL,100 μL/well, Recombinant Human Semaphorin 3F Fc Chimera (Catalog # 9878-S3) binds with an ED50 of 0.1‑0.6 μg/mL.

1 μg/lane of Recombinant Human Semaphorin 3F was resolved with SDS-PAGEunder reducing (R) and non-reducing (NR) conditions and visualized by silverstaining, showing bands at 91 - 125 kDa and 200 - 250 kDa,respectively.

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

Recombinant Human Semaphorin 3F Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Neuropilin‑2 Fc Chimera (Catalog # 2215-N2) is immobilized at 2 μg/mL, 100 μL/well, it binds Recombinant Human Semaphorin 3F Fc Chimera. The concentration of Recombinant Human Semaphorin 3F Fc Chimera that produces 50% of the optimal binding response is 0.1-0.6 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived human Semaphorin 3F protein
  

  Human Semaphorin 3F (Ser19-Gln772) (Leu503Met, Arg585Ala, Arg586Ala, Arg651Ala) Accession # Q13275-1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q13275-1
• N-terminal Sequence: Ser19
• 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: 111 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: 91-125 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 °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 Tris and NaCl with Trehalose.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in water.

Notes

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

Alternate Names for Recombinant Human Semaphorin 3F Fc Chimera Protein, CF

• sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F
• sema domain, immunoglobulin domain (Ig), short basic domain, secreted, 3F
• sema III/F
• sema IV
• Sema3F
• SEMA4
• SEMA-IV
• SEMAK
• Semaphorin 3F
• semaphorin III/F
• semaphorin IV

Background

Semaphorin 3F (Sema 3F; previously Sema IV) is one of six Class 3 (secreted) semaphorins. Class 3 semaphorins are potent chemorepellents that function in axon guidance and/or vascular tip cell guidance during development (1). Sema 3F is expressed in the developing nervous system, especially in the dorsal spinal cord (2, 3). In adults, Sema 3F is expressed in the lung and most other tissues (2). Crystal structures of semaphorins reveal that the 500 amino acid (aa) N-terminal Sema domain forms a seven-blade beta-propeller similar to that found in integrin molecules. Fourteen conserved cysteine residues and one or more N-glycosylation sites are thought to be critical for forming the secondary structure (4). Isoform 2 is missing aa 153-183 within the Sema domain relative to the long form (Isoform 1) but appears to have similar activity. C-terminal to the Sema domain, Sema 3F has a basic domain, a cysteine-knot plexin/semaphorin/integrin (PSI) domain, an Ig-like domain, a cysteine for dimerization and another basic domain at the C-terminus. Dimerization and cleavage at the C-terminus are required for repulsing activity of class 3 semaphorins (5). Human Sema 3F shares 96% aa identity with mouse and rat Sema 3F. Sema 3F signaling is transduced by type-A plexins, especially Plexin-A3, via interaction with neuropilin-2 (3, 6). Sema 3F-Npn-2-Plexin-A3 signaling regulates AMPA-type glutamate receptor (AMPAR) homeostatic downscaling in response to increased neuronal activity of cortical neurons (7). Genetic disruption of either Sema 3F or neuropilin-2 alters motor axon trajectory to the ventral forelimb (3). Sema 3F is deleted or down-regulated in many metastatic tumors such as colorectal cancer, oral squamous carcinoma, lung cancer, and many others (8-10). Restoration of Sema 3F decreases tumorigenicity, vascularization and adhesiveness, most likely through repulsive interactions, VEGF antagonism and downstream integrin regulation (11).

1. Kruger, R.P. et al. (2005) Nature Rev. Mol. Cell Biol. 6:789.
2. Eckhardt, F. and A. Meyerhans (1998) Neuroreport 9:3975.
3. Huber, A.B et al. (2005) Neuron 48:949.
4. Gherardi, E. et al. (2004) Curr. Opin. Struct. Biol. 14:669.
5. Adams, R.H. et al. (1997) EMBO J. 16:6077.
6. Yaron, A. et al. (2005) Neuron 45:513.
7. Wang Q. et al. (2017) Neuron. 96(5):1084.
8. Liu, Y. et al. (2017) Cell Mol Biol Lett. Dec 28; 22:32.
9. Gao, X. et al. (2015) Int J Clin Exp Pathol. 8(10):12766.
10. Potiron, V.A. et al. (2007) Cancer Res. 67(18):8708.
11. Chedotal, A. et al. (2005) Cell Death Differ. 12:1044.

Publications for Semaphorin 3F (9878-S3)(3)

Publications using 9878-S3

• S Dutta, NS Polavaram, R Islam, S Bhattachar, S Bodas, T Mayr, S Roy, SAY Albala, MI Toma, A Darehshour, A Borkowetz, S Conrad, S Fuessel, M Wirth, GB Baretton, LC Hofbauer, P Ghosh, KJ Pienta, DL Klinkebiel, SK Batra, MH Muders, K Datta Neuropilin-2 regulates androgen-receptor transcriptional activity in advanced prostate cancer Oncogene, 2022-06-27;0(0):. 2022-06-27 [PMID: 35754042] (Bioassay, Human)
• MW Tang, B Malvar Fer, SP Newsom, JD van Buul, TRDJ Radstake, DL Baeten, PP Tak, KA Reedquist, S García Class 3 semaphorins modulate the invasive capacity of rheumatoid arthritis fibroblast-like synoviocytes Rheumatology (Oxford), 2018-05-01;0(0):. 2018-05-01 [PMID: 29471421] (Stimulation, Human)
• V Mohan, CS Sullivan, J Guo, SD Wade, S Majumder, A Agarwal, ES Anton, BS Temple, PF Maness Temporal Regulation of Dendritic Spines Through NrCAM-Semaphorin3F Receptor Signaling in Developing Cortical Pyramidal Neurons Cereb. Cortex, 2019-03-01;0(0):. 2019-03-01 [PMID: 29415226] (Bioassay, Mouse)

Bioinformatics

• Uniprot:
  • Q13275-1()