Photo Cross Linkers

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Cross-linking refers to the process of chemically bonding two or more molecules through a covalent bond. The crosslinker comprises a reactive end which is reactive with specific functional groups located on proteins or other molecules, such as primary amines and sulfhydryl groups. Multiple chemical groups on proteins and polypeptides can be used for cross-linking, so proteins and polypeptides can be used as targets for coupling in studies using cross-linking methods.

Application

Cross-linkers are used to determine the relationship between adjacent proteins as well as ligand-receptor interactions. Photo-reactive crosslinkers are widely used for nonspecific bioconjugation. While numerous options exist, the two most common photo-reactive chemical groups are diazirines and aryl-azides. Photo cross linkers are used for the study of protein-protein or protein-oligonucleotide interactions in living cells. They are typically used in the following manner:

Advantages of photo-crosslinking:

Available Services

Creative Peptides is committed in exploiting new technologies and providing comprehensive peptides modification and conjugation services to help our clients with various projects, please contact us for more information and a detailed quote. We have advanced technical support, strong comprehensive strength, rich quality management experience, and huge scale effect. Creative Peptides provides high-quality, low-cost, high-tech peptide products to customers around the world. Every step of peptide synthesis is subject to Creative Peptides’ stringent quality control. Typical delivery specifications include:

References

  1. Hino, N., Okazaki, Y., Kobayashi, T., Hayashi, A., Sakamoto, K., & Yokoyama, S. (2005). Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid. Nature methods, 2(3), 201.,
  2. Kramer, K., Sachsenberg, T., Beckmann, B. M., Qamar, S., Boon, K. L., Hentze, M. W. & Urlaub, H. (2014). Photo-cross-linking and high-resolution mass spectrometry for assignment of RNA-binding sites in RNA-binding proteins. Nature methods, 11(10), 1064.
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