Cap-Clip™ Acid Pyrophosphatase
Cap-Clip™ Acid Pyrophosphatase is a plant-derived enzyme that hydrolyzes various pyrophosphate bonds, including the pyrophosphate bonds of the 5'-terminal m7GpppG "cap" of eukaryotic messenger RNAs.
For the removal of cap structures (decapping) from various RNAs (i.e. mRNAs) resulting in 5'-monophosphate RNAs. Can be substituted unit for unit, into any preexisting protocol for Tobacco Acid Pyrophosphatase (TAP) utilizing the same buffer.
Cap-Clip™ Acid Pyrophosphatase is a plant-derived enzyme that hydrolyzes various pyrophosphate bonds, including the pyrophosphate bonds of the 5'-terminal m7GpppG "cap" of eukaryotic messenger RNAs, as well as 5' cap structures on many small nuclear RNAs (snRNAs), heterogeneous nuclear RNAs (hnRNAs) and some viral RNAs. Complete hydrolysis of such capped RNAs generates RNA that has a 5'-monophosphate group.
Our plant-derived Cap-Clip™ Acid Pyrophosphatase has optimal activity at acidic pH and is supplied with acidic reaction buffer. Therefore it is easy to inactivate the enzyme by addition of alkali in a similar manner to tobacco acid pyrophosphatase making reaction products immediately suitable for downstream applications. In contrast, alternative pyrophosphatases produced in E. coli are active at alkaline pH and need to be inactivated at acidic pH. This necessitates an additional clean-up step for downstream applications making plant-derived Cap-Clip™ Acid Pyrophosphatase the enzyme of choice for many protocols.Cap-Clip™ Acid Pyrophosphatase was developed as an improvement over Tobacco Acid Pyrophosphatase (TAP). Cap-Clip Acid Pyrophosphatase can be used unit for unit in any previously developed protocol that utilized TAP. The Reaction Buffers for the two enzymes are identical. With lot to lot consistency, absence of critical contaminants and a dependable inventory, Cap-Clip Acid Pyrophosphatase replaces all TAP needs.
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