I would like to attach Biotin to peptide (10-mer) or protein and then bind it with Streptaavidin.
Any suhggestions please?
It all depends on the sequence of your peptide, which residue(s) you want to biotinylate, if you need a linker, and other factors. When it comes to protein modification my reference is always Pierce/Thermo
https://www.thermofisher.com/it/en/home/life-science/protein-biology/protein-labeling-crosslinking/protein-labeling/biotinylation.html?gclid=CjwKEAiA6YDBBRDwtpTQnYzx5lASJAC57ObMYe55kijdCmtL8KykQs72rLblG9CEJRiyu-QqyZgGDRoCza7w_wcB&s_kwcid=AL!3652!3!85589465054!b!!g!!_cat:protein%20labeling&ef_id=Vx1hRAAAAQkN6qD9:20161107220525:s
You might be better off having the biotinylation done at the time the peptide is synthesized. This will save you the trouble of having to repurify it after the reaction.
As for the protein, you could chemically biotinylate it on either lysine or cysteine residues. Or you could express it with an avi-tag, purify it and biotinylate it with BirA biotin ligase. Or you could express it with avi-tag in a special strain that causes it to become biotinylated in the cells.
Here is a vendor web site with some useful information about the avi-tag:
http://www.genecopoeia.com/tech/avitag-biotinylation-tag/
Hello Mr. Suresh Pujari ,
Kindly look at the attached documents. I hope, they will be helpful at some extent.
Regards, Babu
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