I have a 1.3kD peptide created for antibody production. I specifically chose this sequence because it is predicted to have good solubility and high antigenicity; however, I'm seeing on a lot of company websites that peptides less than 6-8kD require conjugation to KLH or another larger molecule to induce an antibody response. If my peptide sequence alone should induce an antibody response, is it really necessary to conjugate?
It seems to be generally accepted that you will get a much greater immune response to a conjugate than to the small peptide by itself.
Adam is quite correct, but I'd be tempted to try the unconjugated protein first.
I am too, though it really comes down to a question of money. Two antibody production trials is a lot more expensive than one; however, if I can get enough antibody from even an inferior antigenic response, that would save me some time and money. I'd really like someone's input who has actually tried this before.
Normally, to get a good immune response, you want an immunogen that combines T-cell and B-cell epitopes and optimally shows some multivalence to insure good B-cell activation and internalization for MHC display. In addition, you want a low clearance rate of your immunogen. If your peptide alone gives you good antibody titers, OK. However, chances are that you are getting a poor respons from immunizing with an unconjugated peptide.
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