Recombinant Human Semaphorin 6B Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to cause collapse of chick embryonic dorsal root ganglia (DRG) neuron growth cones. 2.5-5.0 µg/mL of Recombinant Human Semaphorin 6B Fc Chimera causes >50% growth cone collapse in the presence of 10 ng/mL of Recombinant Human beta ‑NGF (Catalog # 256-GF) . Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human Semaphorin 6B protein
Human Semaphorin 6B (Leu26-Ser603) Accession # Q9H3T3
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
63.4 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
110-120 kDa, reducing conditions
Publications
Read Publication using 2094-S6 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 PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 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 6B Fc Chimera Protein, CF
sema domain, transmembrane domain (TM), and cytoplasmic domain, (semaphorin) 6B
Sema6B
SEMAN
Semaphorin 6B
semaphorin VIB
semaphorin Z
semaphorin-6B
semaphorin-6Ba
SEMA-VIB
SEMAZ
SEM-SEMA-Y
UNQ1907/PRO4353
Background
Semaphorin 6B is a member of the class 6 subfamily of semaphorins, a large, highly conserved family of signaling molecules that affect multiple processes including axon guidance, cell migration, synaptogenesis, and dendritic spine formation (1). The class 6 semaphorins are type I transmembrane glycoproteins that contain the characteristic extracellular beta propeller-structured N-terminal semaphorin (sema) domain and also an extracellular plexin-semaphorin-integrin (PSI) domain (2, 3). Additionally, the cytoplasmic domain of Semaphorin 6B contains a proline-rich sequence that has been shown to interact with the SH3 domain of the Src signaling protein (4). Human Semaphorin 6B has a molecular weight of approximately 120 kDa and shares 95% and 94% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively. Full-length Semaphorin 6B is thought to form disulfide-linked homodimers (4). Alternative exon splicing creates a 492 aa isoform that may be secreted (Semaphorin 6B.1) and a 657 aa isoform with a shortened cytoplasmic tail (Semaphorin 6B.2) (5). Semaphorin 6B is highly expressed in heart and brain and is observed in most other tissues at lower levels (5). Semaphorin 6B has also been shown to be highly expressed in human gastric, breast, and glioblastoma cancer cells and is thought to be involved in tumor differentiation and metastasis (5-7). Interestingly, retinoic acid, which slows cancer cell growth, has been shown to down-regulate Semaphorin 6B expression (5, 6). It is hypothesized the retinoid X receptors (RXRs) form heterodimers with peroxisome proliferator-activated receptors (PPARs), which then bind to a putative peroxisome proliferator-responsive element (PPRE) in the SEMA6B promoter region (6, 8, 9). Semaphorin 6B has also been shown to mediate repulsion of mouse sympathetic ganglion axons and hippocampal mossy fibers via binding to the transmembrane protein Plexin A4 (10, 11).
Pasterkamp, R.J. and R.J. Giger (2009) Curr. Opin. Neurobiol. 19:263.
Neufeld, G. et al. (2005) Front. Biosci. 10:751.
Roney, K. et al. (2013) Protein Cell 4:17.
Eckhardt, F. et al. (1997) Mol. Cell. Neurosci. 9:409.
Correa, R.G. et al. (2001) Genomics 73:343.
Murad, H. et al. (2006) Int. J. Oncol. 28:977.
Ge, C. et al. (2013) J. Int. Med. Res. 41:284.
Collet, P. et al. (2004) Genomics 83:1141.
Murad, H. et al. (2011) Mol. Med. Rep. 4:575.
Suto, F. et al. (2005) J. Neurosci. 25:3628.
Tawarayama, H. et al. (2010) J. Neurosci. 30:7049.
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