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Protein phosphorylation is an important covalent post-translational modification that can alter the structural conformation of a protein, which then regulates the function, location and specific binding of the target protein. Many cellular processes are regulated by the reversible phosphorylation of proteins and 30% of the proteins are likely to be phosphorylated at some point during their existence.
Endogenous proteins are produced and degraded in a balanced state, so their cellular levels are stable under stable environmental conditions. Crude cell extracts contain a number of endogenous enzymes, such as phosphatases and proteases, which are capable of degrading and modifying proteins in the extracts. The best way to increase the yield of intact proteins is to add inhibitors of those enzymes known to be present.
Phosphatase Inhibitor Cocktail 2 inhibits tyrosine protein phosphatases, acid and alkaline phosphatases. This phosphatase inhibitor cocktail has been optimized and tested on cell extracts from various animal tissues.
This phosphatase inhibitor cocktail contains individual components, including Sodium orthovanadate, Sodium molybdate, Sodium tartrate, Imidazole and Sodium Fluoride. This phosphatase inhibitor cocktail is supplied as a ready-to-use solution in ddH2O.
Thaw at room temperature, add at 1:100 (v/v) dilution to solution samples (such as cell lysates or tissue extracts) before assaying.
Applications: WB, Co-IP, pull-down, IF, IHC, kinase assay and etc.