Greater than 98.0% as determined by SDS-PAGE.
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.
Recombinant mouse adiponectin is often produced in HEK 293 cells (human embryonic kidney cells) to ensure proper folding and post-translational modifications. The recombinant form typically includes the full-length protein, which ranges from amino acids 18 to 247 . This protein is expressed without any tags to maintain its native structure and function .
Adiponectin is known for its anti-diabetic, anti-atherogenic, and anti-inflammatory activities. It stimulates the phosphorylation and activation of AMP-activated protein kinase (AMPK) in the liver and skeletal muscle, enhancing glucose utilization and fatty acid oxidation . Additionally, adiponectin antagonizes tumor necrosis factor-alpha (TNF-alpha) by negatively regulating its expression in various tissues, including the liver and macrophages .
Due to its beneficial effects on metabolism and inflammation, adiponectin is a potential therapeutic target for treating metabolic disorders such as diabetes, obesity, and cardiovascular diseases. The recombinant form of mouse adiponectin is used in various research applications to study its functions and therapeutic potential.
Recombinant mouse adiponectin is typically stored in a lyophilized form at room temperature. Upon reconstitution in phosphate-buffered saline (PBS), it should be aliquoted and stored at -80°C for long-term use or at +4°C for short-term use. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s stability and activity .