Calcium carbonate/glycine

GSK1016790A is a potent and selective transient receptor potential vanilloid 4 (TRPV4) channel agonist. GSK1016790A can elicit Ca2+ influx and elevate intracellular Ca2+ in HEK cells。.

GSK1016790A is a potent and selective transient receptor potential vanilloid 4 (TRPV4) channel agonist. GSK1016790A can elicit Ca2+ influx and elevate intracellular Ca2+ in HEK cells。.

GSK1016790A is a potent and selective transient receptor potential vanilloid 4 (TRPV4) channel agonist. GSK1016790A can elicit Ca2+ influx and elevate intracellular Ca2+ in HEK cells。.

GSK1016790A is a potent and selective transient receptor potential vanilloid 4 (TRPV4) channel agonist. GSK1016790A can elicit Ca2+ influx and elevate intracellular Ca2+ in HEK cells。.

A potent and ATP-competitive inhibitor of GSK-3 (K i = 24 nM). An aminopyrazole compound that acts as a potent and ATP-binding site inhibitor of GSK-3 with a K i of 24 nM.

A potent and ATP-competitive inhibitor of GSK-3 (K i = 24 nM). An aminopyrazole compound that acts as a potent and ATP-binding site inhibitor of GSK-3 with a K i of 24 nM.

5'-GTP trisodium salt hydrate is an activator of the signal transducing G proteins and also serves as an energy-rich precursor of mononucleotide units in the enzymatic biosynthesis of DNA and RNA.Form:SolidIC50&amp: Target:Human Endogenous

5'-GTP trisodium salt hydrate is an activator of the signal transducing G proteins and also serves as an energy-rich precursor of mononucleotide units in the enzymatic biosynthesis of DNA and RNA.Form:SolidIC50&amp: Target:Human Endogenous

Guanylyl Imidodiphosphate is the preferred GTP analog to activate ADP-ribosylation factor. Guanylyl Imidodiphosphate binds and irreversibly activates G proteins. Since a cycle of GTP binding, hydrolysis, and release is required for the initiation of

GUINEA PIG INTESTINE, Non-sterile, Tissue, No expiration date is given for this product if properly stored.

General DescriptionGVBE is an isotonic buffer used in complement assays to prevent complement activation or to stop ongoing complement activation when added at the end of an incubation (Morgan, B.P. (2000): Dodds, A.W. and Sim, R.B. (1997)).Buffer

General description Shown to inhibit fibronectin function by binding to platelet-binding sites. Biochem/physiol Actions Cell permeable: no Primary Target fibronectin Product does not compete with ATP.