Recombinant Mouse Semaphorin 3A Fc Chimera Protein Summary
Details of Functionality
Measured by its ability to cause collapse of chick embryonic dorsal root ganglia (DRG) neuron growth cones. 20-60 ng/mL of Recombinant Mouse Semaphorin 3A Fc Chimera causes >50% growth cone collapse in the presence 10 ng/mL Recombinant Human beta ‑NGF (Catalog # 256-GF).
Source
Chinese Hamster Ovary cell line, CHO-derived mouse Semaphorin 3A protein
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
110.1 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
115-120 kDa, reducing conditions
Publications
Read Publications using 5926-S3 in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Semaphorin 3A Fc Chimera Protein
(semaphorin) 3A
coll-1
collapsin 1
Hsema-I
Hsema-III
MGC133243
sema domain, immunoglobulin domain (Ig), short basic domain, secreted
Sema III
SEMA1
Sema3A
SEMAD
SEMAIII
SEMAL
Semaphorin 3A
semaphorin D
Semaphorin III
semaphorin L
semaphorin-3A
SemD
Background
Semaphorin 3A (Sema3A; previously sem D, sema III or collapsin) is one of six Class 3 secreted semaphorins which share ~40-50% amino acid (aa) identity (1-3). Class 3 semaphorins are potent chemorepellents that function in axon and/or vascular guidance during development (2, 3). The 772 aa mouse Sema3C contains a 20 aa signal sequence, an ~500 aa N-terminal Sema domain that forms a beta -propeller structure similar to that found in integrin molecules, a PSI domain, a furin-type cleavage site, an Ig-like domain, and a C-terminal basic domain (3, 4). Covalent dimerization plus cleavage at the C-terminus are required for activity of class 3 semaphorins (5, 6). The 95 kDa mature mouse Sema3A shares at least 95% aa identity with human, rat, equine and canine Sema3A, and 90% and 86% aa identity with chick and zebrafish Sema3A, respectively. Type 3 semaphorins transduce signals through transmembrane plexins, either directly or by binding associated neuropilin receptors (3). Sema3A signaling is transduced by plexin A1-4, indirectly via neuropilin-1 (3). Sema3A activity is mediated by small GTPases that influence actin rearrangement and integrin activity (7-9). It is important in developmental organization of central and peripheral nerves, including those in heart, lung, kidneys, bones, teeth, and visual and olfactory systems (1, 2, 10, 11). Gradients of Sema3A repel axons, but attract dendrites (11, 12). Sema3A affect vasculogenesis by inhibiting integrin function and, with Sema3F, promoting apoptosis of endothelial cells (3, 9, 12). It is thought to suppress cancer-related angiogenesis (3). In the immune system, Sema3A influences T cell proliferation, migration, response to activation, and interactions with dendritic cells (7, 13). It negatively regulates platelet activation (14). Expression of Sema3A in relevant parts of the nervous system may be increased in Alzheimer’s disease, multiple sclerosis, ischemia and schizophrenia (2).
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Roth, L. et al. (2009) Cell. Mol. Life Sci. 66:649.
Neufeld, G and O. Kessler (2008) Nat. Rev. Cancer 8:632.
Gherardi, E. et al. (2004) Curr. Opin. Struct. Biol. 14:669.
Adams, R. H. et al. (1997) EMBO J. 16:6077.
Klosterman, A. et al. (1998) J. Biol. Sci. 273:7326.
Lepelletier, Y. et al. (2006) Eur. J. Immunol. 36:1782.
Schlomann, U. et al. (2009) J. Cell Sci. 122:2034.
Serini, G. et al. (2003) Nature 424:391.
Ieda, M. et al. (2007) Nat. Med. 13:604.
Chen, G. et al. (2008) Nat. Neurosci. 11:36.
Guttmann-Raviv, N. et al. (2007) J. Biol Chem. 282:26294.
Lepelletier, Y. et al. (2007) Proc. Natl. Acad. Sci. USA 104:5545.
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