D-myo-Inositol-1,3,4,5,6-pentaphosphate ammonium salt  (Synonyms: Ins(1,3,4,5,6)P5 ammonium salt; 1,3,4,5,6-IP5 ammonium salt)

D-myo-Inositol-1,3,4,5,6-pentaphosphate (ammonium salt) (Ins(1,3,4,5,6)P5 (ammonium salt)) is an isomer of inositol phosphate that acts as a small and soluble second messenger in the transmission of cellular signals. D-myo-Inositol-1,3,4,5,6-pentaphosphate (ammonium salt) can bind to the PH domain of Grp1 with a K_d of 590 nM. D-myo-Inositol-1,3,4,5,6-pentaphosphate (ammonium salt) can inhibit the phosphorylation and kinase activity of Akt/PKB, inducing apoptosis in ovarian, lung, and breast cancer cells. D-myo-Inositol-1,3,4,5,6-pentaphosphate (ammonium salt) exhibits antiangiogenic activity in vitro and blocks capillary tube formation of HUVEC. D-myo-Inositol-1,3,4,5,6-pentaphosphate (ammonium salt) exerts antitumor effects against cancer xenografts in nude mice^{[1][2][3][4][5]}.

750.36

C₆H₄₇N₁₀O₂₁P₅

O[C@@H]1[C@@H]([C@H]([C@@H]([C@H]([C@@H]1OP([O-])([O-])=O)OP([O-])([O-])=O)OP([O-])([O-])=O)OP([O-])([O-])=O)OP([O-])([O-])=O.[NH4+].[NH4+].[NH4+].[NH4+].[NH4+].[NH4+].[NH4+].[NH4+].[NH4+].[NH4+]

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Berridge M. J. (2009). Inositol trisphosphate and calcium signalling mechanisms. Biochimica et biophysica acta, 1793(6), 933–940.  [Content Brief]

  [2]. Majerus P. W. (1992). Inositol phosphate biochemistry. Annual review of biochemistry, 61, 225–250.  [Content Brief]

  [3]. Maffucci, T., et al., (2005). Inhibition of the phosphatidylinositol 3-kinase/Akt pathway by inositol pentakisphosphate results in antiangiogenic and antitumor effects. Cancer research, 65(18), 8339–8349.  [Content Brief]

  [4]. Kavran, J. M., et al., (1998). Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains. The Journal of biological chemistry, 273(46), 30497–30508.Kavran, J. M., et al., (1998). Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains. The Journal of biological chemistry, 273(46), 30497–30508.  [Content Brief]