The protein PRDM9 or PR-domain containing protein 9, plays a major role in localizing meiotic recombination, which reshuffles the genetic material and increases the genetic diversity in populations. However, not much is known about this proteins binding behaviour to the DNA sequence in quantitative terms. This master thesis encompasses the study of the binding affinity and kinetics of murine PRDM9 to its specific target DNA sequences via SPR measurements. To establish and obtain this new data set, multiple preparation steps were done. First, starting with protein expression and purification to obtain a functional and soluble protein. Second, the optimization of DNA synthesis using PCR for DNA amplification and DNA modification. Third, functionality tests of the protein-DNA interaction via Westernblot and EMSA. Forth, the SPR chip setup was optimized for this particular system, and finally, a series of different SPR measurements were performed to gather kinetic binding information on PRDM9-DNA interactions. The results of this master thesis approach a previous paper (Striedner, Schwarz et al. 2017), which demonstrated, that PRDM9 forms a highly stable complex with its binding target with dissociation times of several hours. In this master thesis, a very fast association was observed followed by a very slow dissociation for additional DNA sequences, as well as, other PRDM9 alleles/variants.