Recombinant Human Semaphorin 3F Fc Chimera Protein, CF

R&D Systems | Catalog # 9878-S3

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Key Product Details

  • R&D Systems NS0-derived Recombinant Human Semaphorin 3F Fc Chimera Protein (9878-S3)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

NS0

Accession Number

Q13275-1

Structure / Form

Disulfide-linked homodimer

Applications

Bioactivity
View all Semaphorin 3F Proteins and Enzymes »

Product Specifications

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

Purity

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

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ser19

Predicted Molecular Mass

111 kDa

SDS-PAGE

91-125 kDa, reducing conditions

Activity

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.

Scientific Data Images for Recombinant Human Semaphorin 3F Fc Chimera Protein, CF

Recombinant Human Semaphorin 3F Fc Chimera Protein Binding Activity

Recombinant Human Semaphorin 3F Fc Chimera Protein Binding Activity

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.
Recombinant Human Semaphorin 3F Fc Chimera Protein SDS-PAGE

Recombinant Human Semaphorin 3F Fc Chimera Protein SDS-PAGE

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

Formulation, Preparation, and Storage

9878-S3
Formulation Lyophilized from a 0.2 μm filtered solution in Tris and NaCl with Trehalose.
Reconstitution

Reconstitute at 500 μg/mL in water.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Semaphorin 3F

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).

References

  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.

Alternate Names

Sema3F, SEMA4, SEMAK

Entrez Gene IDs

6405 (Human); 20350 (Mouse); 315996 (Rat)

Gene Symbol

SEMA3F

UniProt

Q13275-1

Additional Semaphorin 3F Products

Product Documents for Recombinant Human Semaphorin 3F Fc Chimera Protein, CF

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Product Specific Notices for Recombinant Human Semaphorin 3F Fc Chimera Protein, CF

For research use only

Related Research Areas

Proteoglycans

Citations for Recombinant Human Semaphorin 3F Fc Chimera Protein, CF

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