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Greene, M.E., Blumberg, B., McBride, O.W., et al. Isolation of the human peroxisome proliferator activated receptor γ cDNA: Expression in hematopoietic cells and chromosomal mapping. Gene Expr 4 281-299 (1995).

Fajas, L., Auboeu, D., Raspé, E., et al. The organization, promoter analysis, and expression of the human PPARγ gene. J Biol Chem 272 18779-18789 (1997).

Elbrecht, A., Chen, Y., Cullinan, C.A., et al. Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors γ 1 and γ 2. Biochem Biophys Res Commun 224 431-437 (1996).

Thuillier, P., Baillie, R., Sha, X., et al. Cytosolic and nuclear distribution of PPARγ2 in differentiating 3T3-L1 preadipocytes. J Lipid Res 39 2329-2338 (1998).

Spiegelman, B.M., and Flier, J.S. Adipogenesis and obesity: Rounding out the big picture. Cell 87 377-389 (1995).

Lemberger, T., Desvergne, B., and Wahli, W. Peroxisome proliferator-activated receptors: A nuclear receptor signaling pathway in lipid physiology. Annu Rev Cell Dev Biol 12 335-363 (1996).

Mukherjee, R., Jow, L., Croston, G.E., et al. Identification, characterization, and tissue distribution of human peroxisome proliferator-activated receptor (PPAR) isoforms PPARγ2 versus PPARγ1 and activation with retinoid X receptor agonists and antagonists. J Biol Chem 272 8071-8076 (1997).

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Description

Antigen:human PPARγ1 amino acids 82-101 (PASPPYYSEKTQLYNKPHEE; amino acids 110-129 of PPARγ2)·Host:rabbit·Application(s):WB·PPARγ is a ligand-activated transcription factor involved in the regulation of lipid homeostasis and may function as a master regulator of adipogenesis.^1,2,3,4 PPARγ mRNA is expressed prominently in adipose tissue, but is also found in large intestine, kidney, liver, and small intestine.⁵ Alternative splicing of the PPARγ gene results in at least two mRNA species that differ at their 5' ends.^1,6 Human PPARγ1 and PPARγ2 proteins are 53 and 57 kDa, respectively, based on the deduced amino acid sequences.⁶ PPARγ2 is the major PPARγ isoform found in both the cytosolic and nuclear fractions of undifferentiated 3T3-L1 cells.⁷ Total cellular PPARγ2 protein increases approximately 2-fold following differentiation of 3T3-L1 cells, whereas only small quantities of PPARγ1 are detected in the nuclear fraction following differentiation.⁷

1Greene, M.E., Blumberg, B., McBride, O.W., et al. Isolation of the human peroxisome proliferator activated receptor γ cDNA: Expression in hematopoietic cells and chromosomal mapping. Gene Expr 4 281-299 (1995).

2Elbrecht, A., Chen, Y., Cullinan, C.A., et al. Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors γ 1 and γ 2. Biochem Biophys Res Commun 224 431-437 (1996).

3Spiegelman, B.M., and Flier, J.S. Adipogenesis and obesity: Rounding out the big picture. Cell 87 377-389 (1995).

4Lemberger, T., Desvergne, B., and Wahli, W. Peroxisome proliferator-activated receptors: A nuclear receptor signaling pathway in lipid physiology. Annu Rev Cell Dev Biol 12 335-363 (1996).

5Fajas, L., Auboeu, D., Raspé, E., et al. The organization, promoter analysis, and expression of the human PPARγ gene. J Biol Chem 272 18779-18789 (1997).

6Mukherjee, R., Jow, L., Croston, G.E., et al. Identification, characterization, and tissue distribution of human peroxisome proliferator-activated receptor (PPAR) isoforms PPARγ2 versus PPARγ1 and activation with retinoid X receptor agonists and antagonists. J Biol Chem 272 8071-8076 (1997).

7Thuillier, P., Baillie, R., Sha, X., et al. Cytosolic and nuclear distribution of PPARγ2 in differentiating 3T3-L1 preadipocytes. J Lipid Res 39 2329-2338 (1998).