I have a tetrapeptide that is biotinylated with a 6-carbon linker between the Biotin moeity and the tetrapeptide. I am trying to use the ligand for receptor characterization. I am trying pulldown and cell histchomestry staining. Could any one suggest to us a reliable method for pulldown and histochemistry? Thanks.
Take a look at these protocols: https://gozani-lab-website.github.io/website/docs/Pull-down-Assay-of-Biotin-labeled-Histone-peptides.pdf. https://www.fishersci.co.uk/webfiles/uk/web-docs/UKLS_1076.PDF.Article Histochemical detection of binding sites for human growth ho...
Hi. I hope the following website could help you:
https://www.sciencedirect.com/topics/neuroscience/biotinylation
Hi,
years ago (Bawolak MT et al., Peptides 2008; 29: 1626), we evaluated 2 bradykinin B2 antagonists N-terminally extended with either biotin of fluorescein. Both had respectable and similar receptor affinities. However, the biotin conjugate did not support B2R epifluorescence microscopy when combined with fluorescent streptavidin, while the fluorescein conjugate worked alone. This was interpreted as steric hindrance between the receptor and streptavidin (a large protein), as a small bifunctional peptide cannot bring the 2 proteins together.
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