D-myo-Inositol-1,3,4,5,6-pentaphosphate (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 Kd 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].

Product Specifications

Product Name Alternative

Ins (1,3,4,5,6) P5 (ammonium salt) ; 1,3,4,5,6-IP5 (ammonium salt)

UNSPSC

12352211

Target

Akt

Related Pathways

PI3K/Akt/mTOR

Field of Research

Cancer

Smiles

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+]

Molecular Formula

C6H47N10O21P5

Molecular Weight

750.36

References & Citations

[1]Berridge M. J. (2009) . Inositol trisphosphate and calcium signalling mechanisms. Biochimica et biophysica acta, 1793 (6), 933–940.|[2]Majerus P. W. (1992) . Inositol phosphate biochemistry. Annual review of biochemistry, 61, 225–250.|[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. |[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.