When Recombinant Human Semaphorin 3B Fc Chimera (Catalog # 9618-S3) is coated at 1 μg/mL, 100 μL/well, it binds to Recombinant Rat Neuropilin‑1 Fc Chimera (Catalog # 566‑N1) with an ED50 of ...read more
Recombinant Human Semaphorin 3B Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Semaphorin 3B Fc Chimera is coated
at 1 μg/mL, 100 μL/well, it binds to
Recombinant
Rat Neuropilin‑1 Fc Chimera (Catalog # 566-N1)
with an ED50 of 25-150 ng/mL.
Source
Trichoplusia ni, T. ni (baculovirus)-derived human Semaphorin 3B protein
Human Semaphorin 3B (Ala25-Gly727(Arg551Ala, Arg554Ala)) Accession # Q13214-1
>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
105 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
96-116 kDa, reducing conditions
Publications
Read Publication using 9518-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.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Citric Acid, NaCl and 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 3B Fc Chimera Protein, CF
(semaphorin) 3B
LUCA-1
Sema A(V)
sema domain, immunoglobulin domain (Ig), short basic domain, secreted
Sema V
SemA
SEMA3B
SEMA5
SEMA5FLJ34863
SEMAA
Semaphorin 3B
semaphorin A
semaphorin V
semaphorin-3B
semaphorin-V
SEMAV
Background
Semaphorin 3B (Sema3B), also known as Semaphorin V and Sema A(V), is an approximately 90 kDa member of the semaphorin family that plays a role in cancer, neuronal and
vascular development (1-4). Class 3 semaphorins are secreted molecules found in
vertebrates and contain a common domain structure. The Sema3B domains consist
of a 484 aa Sema domain, followed by a plexin-semaphorin-integrin (PSI) domain,
an 87 aa Ig-like C2-type domain, and a 21 aa basic domain (5). Within these
domains, human Sema3B shares 88% and 90% aa sequence identity with mouse and
rat Sema3B, respectively. Like other Class 3 semaphorins, Sema3B signaling is
transduced by a transmembrane plexin-A dimer, which also has a Sema domain and
is coupled to kinase pathways (6, 7). Sema3B binds indirectly to plexins, and
requires interaction with neuropilins for activity (6, 7). Repulsive signals
through Neuropilin-1 (Npn-1) and attractive signals through Neuropilin-2
(Npn-2) have been identified, affecting adhesion molecule activity in opposite
directions (6, 8). In tumors, Sema3B competes with VEGF165 for binding to
Npn-1, which in part down-regulates tumor angiogenesis, inhibits tumor cell
proliferation and promotes apoptosis (9, 10). However, it is also proposed to
promote dissemination and metastatic progression by stimulating Npn-1 mediated
IL-8 secretion in a subset of tumors that over-express Sema3B (11). In
differentiating osteoblasts, Sema3B expression is induced by vitamin D and
promotes osteoclastogenesis (12).
Sekido, Y. et al. (1996) Proc Natl Acad Sci U S A. 93:4120.
Gu, C. and E. Giraudo. (2013) Exp. Cell Res. 319:1306.
Sabag, A. et al. (2012) PLoS One. 7:e42912.
Aghajanian, H. et al. (2014) J. Biol. Chem. 289:17971.
Yazdani, U. and J. Terman. (2006) Genome Biology. 7:211.
Halloran, M. C. and M. A. Wolman (2006) Curr. Opin. Cell Biol. 18:533.
Neufeld, G. and O. Kessler (2008) Nat. Rev. Cancer 8:632.
Falk, J. et al. (2005) Neuron 48:63.
Castro-Rivera, E. et al. (2004) Proc. Natl. Acad. Sci. USA 101:11432.
Koyama, N. et al. (2008) Oncogene 27:6581.
Rolny, C. et al. (2008) J. Exp. Med. 205:1155.
Sutton, A. L. M. et al. (2008) Mol. Endocrinol. 22:1370.
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