The classical antibody development process often requires the expression of recombinant proteins, but full-length expression of certain proteins, especially multi-transmembrane GPCR proteins and ion channel proteins, is very difficult, whereas antibodies generated by DNA immunization have a much higher probability of recognizing conformational epitopes of the proteins, mainly due to the fact that the exogenous genes can be directly expressed and synthesized in vivo to synthesize full-length proteins with their natural conformations, thereby eliciting the corresponding immune response.

1. No need to express or purify antigens (especially certain pathogenic antigens), avoiding biosafety issues

2. Test the immunization effect of different antigen sequences efficiently.

3. Rapid development of antibodies against certain outbreaks of infectious diseases once the gene sequences have been identified.

4. Antibodies can be developed for conformational epitopes.

5. Wide range of hosts for immunization, including rats, mice, guinea pigs, and New Zealand white rabbits, etc.

Immunization Procedure for Mouse Tail Vein Injection