Recombinant Human Semaphorin 3D Fc Chimera Protein, CF Summary
|Human Semaphorin 3D |
(Thr37-His736 (Arg571Ala) & (Arg572Ala))
Accession # O95025
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in Tris and NaCl with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in water.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: Semaphorin 3D
Semaphorin 3D (Sema3D) is a member of the semaphorin family that plays a role in neuronal and vascular development (1, 2). Class 3 semaphorins are secreted molecules, and contain a common domain structure. The human Sema3D domains consist of a 488 amino acid (aa) Sema domain, a 53 aa plexin-semaphorin-integrin (PSI) domain, an 89 aa Ig-like C2-type domain, and a 35 aa basic domain which is proteolytically processed (3, 4). Within these domains, human Sema3D shares 94% aa sequence identity with mouse and rat Sema3D. Sema3D induces the collapse and paralysis of neuronal growth cones and promotes fasciculation of axons (5, 6). Sema3D also inhibits endothelial cell motility and tubulogenesis through cytoskeletal reorganization (2). Binding to Neuropilin-I is required for Sema3D signaling (7). ErbB2 was shown to be a potential Sema3D co-receptor, which is phosphorylated in response to Sema3D in HUVEC cells (7). Sema3D inhibition of vascular development facilitates inhibition of glioblastoma growth in the cortex of the brain (1).
- Sabag, A. et al. (2012) PLoS One. 7:e42912.
- Aghajanian, H. et al. (2014) J. Biol. Chem. 289:17971.
- Takahashi, K. et al. (2009) Biochimica et Biophysica Acta. 1790:395.
- Gu, C. and E. Giraudo. (2013) Exp. Cell Res. 319:1306.
- Kuhn, T.B. et al. (2000) J. Neurobiology. 44:126.
- Wolman, M.A. et al. (2007) J. Neurobiology. 27:9653.
- Aghajanian, H. et al. (2015) Nature Commun. 7:12038.
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