The human PPARγ gene was characterized, including its structure, promoters, and tissue-specific expression. Two PPARγ isoforms, PPARγ1 and PPARγ2, were identified in humans, with PPARγ1 being more abundant than PPARγ2 in most tissues. PPARγ1 was highly expressed in adipose tissue and large intestine, while PPARγ2 was less abundant. PPARγ2 was barely detectable in skeletal muscle. The human PPARγ gene consists of nine exons and spans over 100 kb of genomic DNA. Alternate transcription start sites and splicing generate PPARγ1 and PPARγ2 mRNAs, which differ at their 5'-ends. PPARγ1 is encoded by eight exons, and PPARγ2 by seven exons. The 5'-untranslated region of PPARγ1 is encoded by exons A1 and A2, while that of PPARγ2 and its N-terminal amino acids are encoded by exon B. The remaining six exons are common to both isoforms. PPARγ is activated by thiazolidinediones and prostaglandin J2 and binds to a PPRE. The PPARγ gene structure was determined, and its expression pattern and regulatory factors were studied. PPARγ plays a central role in adipocyte differentiation, with PPARγ1 being the predominant isoform in human tissues. PPARγ2 is involved in adipocyte differentiation, and its expression is regulated by transcription factors such as C/EBPβ and δ. PPARγ is also expressed in the large intestine, suggesting a role in colonic function. The PPARγ gene is highly conserved between humans and mice, with similar structures and transactivation functions. The findings provide insights into the regulation of PPARγ expression and its role in metabolic disorders. The structure of the PPARγ gene will facilitate the study of mutations in humans, while understanding its expression patterns and regulatory factors is crucial for understanding PPAR biology.The human PPARγ gene was characterized, including its structure, promoters, and tissue-specific expression. Two PPARγ isoforms, PPARγ1 and PPARγ2, were identified in humans, with PPARγ1 being more abundant than PPARγ2 in most tissues. PPARγ1 was highly expressed in adipose tissue and large intestine, while PPARγ2 was less abundant. PPARγ2 was barely detectable in skeletal muscle. The human PPARγ gene consists of nine exons and spans over 100 kb of genomic DNA. Alternate transcription start sites and splicing generate PPARγ1 and PPARγ2 mRNAs, which differ at their 5'-ends. PPARγ1 is encoded by eight exons, and PPARγ2 by seven exons. The 5'-untranslated region of PPARγ1 is encoded by exons A1 and A2, while that of PPARγ2 and its N-terminal amino acids are encoded by exon B. The remaining six exons are common to both isoforms. PPARγ is activated by thiazolidinediones and prostaglandin J2 and binds to a PPRE. The PPARγ gene structure was determined, and its expression pattern and regulatory factors were studied. PPARγ plays a central role in adipocyte differentiation, with PPARγ1 being the predominant isoform in human tissues. PPARγ2 is involved in adipocyte differentiation, and its expression is regulated by transcription factors such as C/EBPβ and δ. PPARγ is also expressed in the large intestine, suggesting a role in colonic function. The PPARγ gene is highly conserved between humans and mice, with similar structures and transactivation functions. The findings provide insights into the regulation of PPARγ expression and its role in metabolic disorders. The structure of the PPARγ gene will facilitate the study of mutations in humans, while understanding its expression patterns and regulatory factors is crucial for understanding PPAR biology.