Human Semaphorin 3E Antibody Summary
Thr25-Ser775 (Arg557Ala and Arg560Ala)
Accession # O15041
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Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Semaphorin 3E in Human T Cells by Flow Cytometry. Human T cells were treated for 3‑5 days with 1 µg/mL PHA then stained with Mouse Anti-Human Semaphorin 3E Monoclonal Antibody (Catalog # MAB32391, filled histogram) or isotype control antibody (Catalog # MAB002, open histogram), followed by Phycoerythrin-conjugated Anti-Mouse IgG F(ab')2Secondary Antibody (Catalog # F0102B). To facilitate intracellular staining, cells were fixed with paraformaldehyde and permeabilized with saponin.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Semaphorin 3E
Semaphorin 3E (Sema3E; previously SemaH) is a 90-95 kDa member of the Class 3 (secreted) semaphorins which, in human, share 40-50% amino acid (aa) sequence identity. Class 3 semaphorins are potent chemorepellents that function in axon guidance and/or vascular tip cell guidance during development (1). Sema3E is highly expressed in developing somites, where it acts as a repulsive cue for PlexinD1-expressing endothelial cells of adjacent intersomitic vessels (2, 3). Crystal structures of semaphorins reveal that the 500 aa N-terminal Sema domain forms a seven-blade beta -propeller similar to that found in integrin molecules. This is accompanied by 14 conserved cysteine residues and one or more N-glycosylation sites are thought critical for forming the secondary structure (4). C-terminal to the Sema domain, Sema3E has a consensus sequence for furin cleavage which, when used, creates a 61 kDa form that does not dimerize, and is highly expressed in tumor cell lines with metastatic potential (5, 6). Further C-terminal are a cysteine-knot plexin/semaphorin/integrin (PSI) domain, an Ig-like domain, a cysteine for dimerization and a basic domain containing another furin cleavage site. Dimerization and cleavage at the C-terminal site are required for repulsing activity of class 3 semaphorins (7). Human Sema3E shares 90%, 85% and 57% aa sequence identity with mouse, bovine and canine Sema3E, respectively. Like other semaphorins, Sema3E signaling is transduced by a transmembrane Plexin dimer, which also has a Sema domain and is coupled to kinase pathways. Unlike other Class 3 semaphorins, Sema3E binds directly to its plexin and does not require interaction with a neuropilin for activity (7). Genetic disruption of either Sema3E or PlexinD1 creates mouse mutants with excessive and disorganized vascular growth and branching, indicating the importance of this ligand-receptor pair for vascular guidance (3, 8).
- Eichmann, A. et al. (2005) Genes Dev. 19:1013.
- Cohen, S. et al. (2005) Eur. J. Neurosci. 21:1767.
- Gu, C. et al. (2005) Science 307:265.
- Gherardi, E. et al. (2004) Curr. Opin. Struct. Biol. 14:669.
- Christensen, C. et al. (1998) Cancer Res. 58:1238.
- Christensen, C. et al. (2005) Cancer Res. 65:6167.
- Adams, R. H. et al. (1997) EMBO J. 16:6077.
- Gitler, A. D. et al. (2004) Dev. Cell 7:107.
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