Recombinant Human Semaphorin 3A Fc Chimera Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Rat Neuropilin-1 Fc Chimera (Catalog # 566-N1) is coated at 2 µg/mL, Recombinant Human Semaphorin 3A Fc Chimera (Catalog # 1250-S3) binds with an ED 50 = 50-300 ng/mL. Measured by its ability to cause collapse of chick embryonic dorsal root ganglia (DRG) neuron growth cones. 20-60 ng/mL of Recombinant Human Semaphorin 3A Fc Chimera causes >50% growth cone collapse in the presence 10 ng/mL Recombinant Human beta -NGF (Catalog # 256-GF). |
| Source |
Mouse myeloma cell line, NS0-derived human Semaphorin 3A protein | Met-6-His tag | Human Semaphorin 3A Lys26-Val771 (Arg552Ala & Arg555Ala) Accession # Q14563 | DIEGRMD | Human IgG 1 (Pro100-Lys330) | N-terminus | | | C-terminus | |
| Accession # |
|
| N-terminal Sequence |
Met & Ser770 |
| Structure / Form |
Disulfide-linked homodimer |
| Protein/Peptide Type |
Recombinant Proteins |
| Gene |
SEMA3A |
| 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 |
|
| Theoretical MW |
113.5 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 |
120 kDa, 90 kDa and 37 kDa, reducing conditions |
| Publications |
Read Publications using 1250-S3 in the following applications:
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Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution. |
| Buffer |
Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and Tween® 20. |
| Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 250 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 3A Fc Chimera Protein, CF
Background
The Semaphorins constitute a large family of secreted, GPI-anchored and transmembrane cell signaling molecules. Depending on their domain organization and species origin, these proteins can be classified into eight groups. To date, at least 19 vertebrate Semaphorins belonging to five groups (class 3 through 7) have been identified. All Semaphorins contain a conserved, 500 amino acid (aa) Sema domain at the amino terminus. Semaphorins are best known for their roles in axon guidance during neuronal development. Semaphorins are also expressed in non-neuronal tissues and are involved in angiogenesis, hematopoiesis, organogenesis, and the regulation of immune functions (1, 2). Class 3 Semaphorins (Sema3) are secreted proteins containing a Sema domain, an immunoglobulin c2-like domain and a basic domain near the carboxyl tail. Sema3A (also referred to as SemaIII, SemD and Collapsin) cDNA predicts a 771 aa precursor protein with a putative 25 aa signal peptide (1-3). Bioactive Sema3A is a disulfide-linked dimer (4). The bioactivity is increased after proteolytic processing by a furin-like endoprotease near the carboxy-terminus (1). The functional receptor complex for Sema3 is composed of two distinct transmembrane proteins: Neuropilin-1 (Npn-1) and Plexin-A. Npn-1 binds directly to Sema3A with high-affinity and confers specificity. Plexin-A interacts with Npn-1 to increase the affinity of the complex for Sema3A and serves as the signaling subunit in the receptor complex (1, 2, 5).
- Nakamura, F. et al. (2000) J Neurobiol. 44:219.
- Goshima, Y. et al. (2002) J. Clin. Invest. 109:993.
- Kolodkin, A.L. et al. (1993) Cell 75:1389.
- Koppel, A.M. et al. (1998) J. Biol. Chem. 273:15708.
- Yu, T.W. et al. (2001) Nature Neurosci. Supplement 4:1169.
- Luo Y. et al. (1993) Cell 75:217.
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