Human elongator protein 3 (hElp3), the catalytic subunit of the multi-subunit elongator complex associating with an RNA polymerase II holoenzyme engaged in transcriptional elongation, was first identified by its acetyltransferase activity, and subsequent data have provided further evidence that the enzyme is involved in histone acetylation and transcription. Variants of Elp3 gene are associated with many human diseases. In order to study the function of Elp3 by chromatin immunoprecipitation (ChIP) and other techniques, we amplified the fragment of hElp3 gene encoding 69 amino acids in the N-terminal of yElp3 from pYES2-hElp3 template and inserted into the prokaryotic expression vector pMXB10 to construct the recombinant plasmid pMXB10-hElp3-N. After inducing the fusion protein expression in E.coli BL21 (DE3) by IPTG, a 36 kD intein-yElp3 fusion protein was obtained. Then the protein was purified by chitin affinity column and used to immune rabbits for acquiring antiserum. The results of ELISA and Western blot indicated that the polyclonal antibody was of high titration and specificity. ChIP assay with this antibody showed that hElp3 exerted the transcriptional regulatory function directly through its binding to the SSA3 promoter and ORF region in yeast，suggesting that it may rescue the delay activation of SSA3 in elp3Δ cells.