Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.
Peroxisome proliferators, recognized as non-genotoxic carcinogens, are believed to influence cellular processes through their interactions with specific nuclear hormone receptors known as peroxisome proliferator-activated receptors (PPARs). These receptors belong to a family of ligand-dependent intracellular proteins that regulate gene expression. Upon activation by specific ligands, PPARs bind to particular DNA sequences, thereby stimulating the transcription of target genes. Research suggests that PPARs can be activated by various peroxisome proliferators, including clofibric acid, nafenopin, and WY-14,643, as well as certain fatty acids.
The antibody solution has a concentration of 1mg/ml and is buffered in a solution of phosphate-buffered saline (PBS) at a pH of 7.4. It also contains 10% glycerol and 0.02% sodium azide as preservatives.
This antibody has undergone rigorous testing in various applications, including ELISA, Western blot analysis, Flow cytometry, and ICC/IF, to ensure its specificity and reactivity. However, it's important to note that optimal antibody dilutions may vary depending on the specific application, and titration experiments are recommended for each investigation to determine the most effective working concentration.
Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.
PPARG antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
PAT4F5AT
Anti-human PPARG mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PPARG protein 209-477 amino acids purified from E. coli.
Mouse IgG1 heavy chain and k light chain.
PPARγ exists in two main isoforms: PPARγ1 and PPARγ2. PPARγ1 is expressed in various tissues, including adipose tissue, colon, and macrophages, while PPARγ2 is predominantly found in adipose tissue and the intestine . These isoforms arise from alternative splicing of the PPARG gene, which is located on chromosome 3 in humans .
PPARγ is a key regulator of adipocyte differentiation and glucose homeostasis. It controls the peroxisomal beta-oxidation pathway of fatty acids by modulating the transcription of target genes such as acyl-CoA oxidase . PPARγ activation enhances lipid uptake and adipogenesis in fat cells, thereby increasing insulin sensitivity and reducing lipotoxicity . Additionally, PPARγ plays a role in inflammatory processes and has been implicated in the pathology of diseases such as obesity, diabetes, atherosclerosis, and cancer .
Mouse anti-human PPARγ antibodies are monoclonal antibodies produced by immunizing mice with human PPARγ protein. These antibodies are used in various research applications, including Western blotting, immunohistochemistry, and flow cytometry, to detect and quantify PPARγ expression in human tissues and cells. They are valuable tools for studying the role of PPARγ in different biological processes and disease states.
PPARγ agonists, such as thiazolidinediones, are used clinically to improve insulin sensitivity in patients with type 2 diabetes. These drugs activate PPARγ, leading to enhanced glucose uptake and reduced blood glucose levels . However, PPARγ activation can also have side effects, including weight gain and fluid retention . Research is ongoing to develop more selective PPARγ modulators with fewer adverse effects.