- The Temptation to Clear Enzymes.

Why Clear Proteases and Phosphatases from Proteins?

In a state of equilibrium, endogenous proteins are produced and degraded, maintaining their cellular levels stable. When proteins are extracted from cells and tissues in vitro, numerous endogenous enzymes capable of degrading the extracted proteins, such as phosphatases and proteases, are also released. With the production of proteins significantly inhibited and degradation continuing, these enzymes can rapidly degrade the proteins in the extract. To prevent the destruction of the target protein by proteases during protein purification, protease inhibitors are added to inhibit their activity.

Additionally, protein phosphorylation and dephosphorylation in cells are the regulatory switches for many important biological activities such as signal transduction, cell proliferation, cell differentiation, and cell apoptosis. Protecting the phosphorylation state of proteins is crucial in the study of protein phosphorylation pathways and signal transduction routes. Therefore, controlling the action of phosphatases is of significant physiological importance in protein research.

Yeasen Biotech continuously innovates and, through the directed design of protein molecular structures and large-scale enzyme protein mutagenesis screening, provides customers with high-performance protease and phosphatase inhibitor products.

Product Introduction

Proteolytic inhibitors (protease inhibitors) broadly refer to substances that bind to certain groups on the active center of protease molecules, reducing their activity or even eliminating it without causing denaturation of the enzyme protein. Substances such as leupeptin, antipain, chymostatin, elastatinaldehyde, aprotinin, and phosphoramidon, which are isolated from actinomycete fermentation broths, can inhibit trypsin, papain, chymotrypsin, elastase, pepsin, and metalloproteinases, respectively, and are all considered protease inhibitors.

Product Composition

Product Information

Different types of protein extracts contain different types of proteases. For example, mammalian cell extracts typically contain a high abundance of serine proteases, bacterial cell extracts usually contain more serine proteases and metalloproteinases, and plant extracts often contain a large number of serine and cysteine proteases, as well as some with aspartic proteases. Additionally, AEBSF can cause mass spectrometry peak drift, so protease inhibitors containing AEBSF are not suitable for mass spectrometry (Mass Spectrometry, MS) detection and analysis. Therefore, Yeasen Biotech offers different types of proteases, phosphatase, and inhibitor mixtures for selection, tailored to the protein extraction and subsequent experimental purposes of different types of samples. Specific purchase information can be found in the order details.

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