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In vitro transcription of capped mRNA with modified nucleotides and Poly(A) tail
TSA (Tyramide Signal Amplification), used for signal amplification of ISH, IHC and IC etc.
Separation of phosphorylated and non-phosphorylated proteins without phospho-specific antibody
A convenient and sensitive way for cell proliferation assay and cytotoxicity assay
Protect the integrity of proteins from multiple proteases and phosphatases for different applications.
Trypsin is a serine protease that hydrolyses proteins in the digestive system of various vertebrates. Pancreas produces trypsin as inactive proenzyme trypsinogen. Active trypsin cleaves peptide chains predominantly at the carboxyl side of the amino acids (lysine or arginine). In the Trypsin Activity Colorimetric Assay, trypsin cleaves a substrate to produce p-nitroaniline (p-NA) that is detectable at λ = 405 nm. Trypsin activity can be measured as the color intensity is proportional to p-NA content. The kit detection limit is 10-100 mU (p-NA unit) trypsin in different samples.