Adiponectin (CT) Blocking Peptide
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Antibody DetailsProduct DetailsReactive Species Human Product Concentration 0.2 mg/ml Amino Acid Location 15 amino acids near the carboxy-terminus of human adiponectin. Formulation This peptide is formulated in PBS pH 7.2 (0.01 M Sodium Phosphate, 0.13 M NaCl) containing 0.1% bovine serum albumin and 0.02% sodium azide. Storage and Handling Store this peptide in working aliquots at -20°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. Country of Origin USA Shipping Next Day Ambient Amino Acid Sequence 15 amino acids near the carboxy terminus of human adiponectin. Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change. DescriptionBackground Adiponectin, also known as Acrp30, is an adipocyte-derived protein with wide ranging paracrine and endocrine effects on metabolism and inflammation. It is induced during adipocyte differentiation, and its secretion is stimulated by insulin. It promotes adipocyte differentiation, fatty acid catabolism, and insulin sensitivity and is negatively correlated with obesity, type 2 diabetes, and atherogenesis. In this context, Adiponectin is an anti-inflammatory agent, but it exerts pro-inflammatory effects in nonmetabolic disorders such as rheumatoid arthritis and inflammatory bowel disease. Adiponectin interacts with the receptors AdipoR1 and AdipoR2, calreticulin, and Cadherin-13/T-Cadherin, as well as with several growth factors. Mature human Adiponectin shares 83% and 85% amino acid (aa) sequence identity with mouse and rat Adiponectin, respectively. The glycosylation of four hydroxylated lysine residues in the collagenous domain is required for the intracellular formation of HMW complexes. The various multimeric forms of Adiponectin exhibit distinct tissue specific and gender specific profiles and activities.
Adiponectin peptide is applicable as a control peptide for blocking antibody binding in Western blotting. References & Citations1. Kim D-H, Sarbassov DD, Ali SM, et al. GβL, a positive regulator of the Rapamycin-sensitive pathway required for the nutrient-sensitive interaction between Raptor and mTOR. Mol. Cell 2003; 11:895-904.
2. Shamji AF, Ngheim P, and Schreiber SL. Integration of growth factor and nutrient signaling: implications for cancer biology. Mol. Cell 2003; 12:271-80.
3. Fingar DC and Blenis J. Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression. Oncogene 2004; 23:3151-71. |
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Products are for research use only. Not for use in diagnostic or therapeutic procedures.