Biotinylated Proteins
Biotinylation is the process of covalently attaching biotin to a molecule, such as amino acid or protein. Generally, Biotinylation is rapid, specific and is unlikely to disturb the natural function of the molecule owing to the small size of biotin. Biotinylation is widely used in biomedical sciences since biotin binds to streptavidin/avidin with an extremely high affinity, fast on-rate, and high specificity. Significantly, biotinylated proteins are widely used as a molecular tool in biotechnological applications. Avi-tag is a small synthetic 15-amino-acid peptide which is effectively biotinylated by BirA, the E. coli biotin ligase, in vitro or in vivo. Avi-Tag can be translationally fused at the N or C terminus of proteins to produce biotin-tagged proteins for isolating protein or labeling for microscopy.
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Biotinylated Recombinant Proteins (1116)
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.
