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PROS-001A
Prosaptide TX14(A)
Thr-D-Ala-Leu-Ile-Asp-Asn-Asn-Ala-Thr-Glu-Glu-Ile-Leu-Tyr
Thr-D-Ala-Leu-Ile-Asp-Asn-Asn-Ala-Thr-Glu-Glu-Ile-Leu-Tyr
Size：1
P1(RMB)：370
MW：1579.7
One letter sequence：TaLIDNNATEEILY
Molecular Formula：C69H110N16O26
Description：This 14-mer prosaptide sequence is derived from the active neurotrophic region in the amino-terminal portion of the saposin C domain. Synthetic peptides derived from this region are biologically active and are named “prosaptides.” Prosaposin and prosaptides are active on a variety of neuronal cells, stimulating sulfatide synthesis and increasing sulfatide concentration in Schwann cells and oligodendrocytes. This indicates that prosaposin and prosaptides are trophic factors for myelin formation.
Literature Reference：Campana, M. et al. FASEB J. 12, 307 (1998); Hiraiwa, M. et al. Proc. Natl. Acad. Sci. USA 94, 4778 (1997); Taylor, E. et al. Pharmacol. 295, 190 (2000); Calcutt, NA. et al. Anesthesiology 93, 1271 (2000).
Cas：
P1(RMB)：370
MW：1579.7
One letter sequence：TaLIDNNATEEILY
Molecular Formula：C69H110N16O26
Description：This 14-mer prosaptide sequence is derived from the active neurotrophic region in the amino-terminal portion of the saposin C domain. Synthetic peptides derived from this region are biologically active and are named “prosaptides.” Prosaposin and prosaptides are active on a variety of neuronal cells, stimulating sulfatide synthesis and increasing sulfatide concentration in Schwann cells and oligodendrocytes. This indicates that prosaposin and prosaptides are trophic factors for myelin formation.
Literature Reference：Campana, M. et al. FASEB J. 12, 307 (1998); Hiraiwa, M. et al. Proc. Natl. Acad. Sci. USA 94, 4778 (1997); Taylor, E. et al. Pharmacol. 295, 190 (2000); Calcutt, NA. et al. Anesthesiology 93, 1271 (2000).
Cas：
