10006373  S1P3 Polyclonal Antibody

Sphingosine-1-phosphate Receptor 3; S1PR3; EDG-3

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Chemical structure definitions are available for many Cayman products. See Chemical Structure Database for details.

Antigen: human S1P3 amino acids 12-25 (VRGNETLREHYQYV) · Host: rabbit · Application(s): WB and ICC; other applications not tested · Sphingosine-1-phosphate (S1P) exerts its activity by binding to five distinct G-protein-coupled receptors, S1P1/EDG-1, S1P2/EDG-5, S1P3/EDG-3, S1P4/EDG-6, and S1P5/EDG-8.1,2 S1P3 couples to Gi/o-ERK, Gq-PLC, and G12/13-Rho axes to mediate S1P-induced cell proliferation, survival, migration, and related signaling events.1,2,3 S1P3 is widely expressed in various tissues, suggesting diverse physiological functions of this receptor.4 The human and murine S1P3 have 378 amino acids with an estimated molecular weight of 42 kDa. Glycosylation at the N-terminal extracellular domain may cause the protein to migrate at different positions in SDS-PAGE. Cayman’s S1P3 polyclonal antibody detects the receptor at 47 kDa using samples from human cerebral cortex. Liver and heart tissues display 2-3 bands between 40-50 kDa, possibly due to different degree of glycosylation.
1  Takuwa, Y., Takuwa, N., Sugimoto, N. The Edg family G protein-coupled receptors for lysophospholipids: Their signaling properties and biological activities. J Biochem 131 767-771 (2002).
2  Ishii, I., Fukushima, N., Ye, X., et al. Lysophospholipid receptors: Signaling and biology. Annu Rev Biochem 73 321-354 (2004).
3  Kluk, M.J., Hla, T. Signaling of sphingosine-1-phosphate via the S1P/EDG-family of G-protein-coupled receptors. Biochim Biophys Acta 1582 72-80 (2002).
4  Takuwa, Y. Subtype-specific differential regulation of Rho family G proteins and cell migration by the Edg family sphingosine-1-phosphate receptors. Biochem Biophys Acta 1582 112-120 (2002).


Purchase 10006373 S1P3 Polyclonal Antibody

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Warning This product is not for human or veterinary use.

Pricing updated 2010-03-20.
Prices are subject to change without notice.

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