Adiponectin (mouse, recombinant)

Adiponectin is a pleiotropic adipokine and homolog of the complement 1q (C1q) family encoded by Adipoq in mice.^1,2 It is composed of an N-terminal signal sequence, a hypervariable region, a collagenous domain, and a C-terminal C1q-like globular domain. It is produced in adipocytes, where the 26.4 kDa monomeric protein is post-translationally modified to induce formation of trimer, hexamer, and high molecular weight (HMW) octadecamers that circulate in serum. These adiponectin multimers have distinct biological activities and do not interconvert once present in the circulation. Plasma levels of adiponectin are decreased in ob/ob mice and mice with diet-induced obesity that have insulin resistance, and exogenous administration of adiponectin improves insulin sensitivity in these mice by increasing β-oxidation in the skeletal muscle and reducing hepatic and musculoskeletal triglyceride content.¹ Chronic administration of adiponectin reduces hyperglycemia, hyperinsulinemia, and body weight in a mouse model of high-fat diet-induced obesity. Cayman's Adiponectin (mouse, recombinant) protein consists of 241 amino acids, has a calculated molecular weight of 26.4 kDa, and a predicted N-terminus of Glu18 after signal peptide cleavage.

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1. Fang, H., and Judd, R.L. Adiponectin regulation and function. Compr. Physiol. 8(3), 1031-1063 (2018).

2. Suzuki, S., Wilson-Kubalek, E.M., Wert, D., et al. The oligomeric structure of high molecular weight adiponectin. FEBS Lett. 581(5), 809-814 (2007).