Protease Inhibitors
Many biological functions rely upon proteases, including food digestion, lysosomal degradation, and signaling cascades. Since proteases trigger an irreversible event, the hydrolysis of a protein, their activity must be tightly controlled. An extensive regulatory network of protease inhibitors has evolved to ensure targeted spatial and temporal control of their activity. Naturally occurring protease inhibitors (antiproteases) are usually proteins or peptides, which control proteolysis within an organism, as well as inactivate proteases of competing or predatory species. Protease inhibitors can be further classified into 5 groups (serine, threonine, cysteine, aspartyl and metalloprotease inhibitors) according to the mechanism employed at the active site of proteases they inhibit. Some protease inhibitors interfere with more than one type of protease. For example, the serine family of protease inhibitors (serpins) is generally known as active against serine proteases, but serpins that inhibit caspases and papain-like cysteine proteases have also been identified.
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Protease Inhibitors Recombinant Proteins (136)
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Recombinant Protein Expression Service
- Codon Optimization
- Gene Synthesis
- Construction of Expression Vector
- Strain Screening
- Protein Expression
- Purification & QC
- Protein Delivery
- Formula: Human
- Molecular Weight: Sf9 insect cells
The EpCAM/TROP1 protein serves as an important homogeneous interacting molecule that promotes direct contact between intestinal epithelial cells (IEC) and intraepithelial lymphocytes (IEL) in the mucosal epithelium. This feature helps establish an immune barrier against mucosal infections. EpCAM/TROP1 Protein, Human (His-SUMO) is the recombinant human-derived EpCAM/TROP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
