Cayman Cardiotrophin-1 (human, recombinant)

Cardiotrophin-1 is a glycosylated polypeptide and member of the IL-6 family of cytokines.¹ It is composed of four α-helices but lacks the hydrophobic N-terminal secretion signal sequence that most IL-6 family proteins contain.² Cardiotrophin-1 is primarily expressed in embryonic and adult cardiomyocytes, but it is also expressed in skeletal muscle, as well as the liver, lungs, and kidneys.^1,3 Its expression is increased under cellular stress conditions, such as hypoxic stress.¹ Cardiotrophin-1 forms a heterocomplex with gp130 and leukemia inhibitory factor receptor β (LIFRβ) in cardiomyocytes and, in other cells, with gp130, LIFRβ, and cytokine-specific α-chains, which signal through the JAK/STAT, ERK/MAPK, and PI3K/AKT pathways. It induces cardiomyocyte hypertrophy in vitro, and levels of cardiotrophin-1 are increased in the heart in animal models after myocardial infarction and protect the heart from ischemic injury.¹ Serum levels of cardiotrophin-1 are increased in patients with heart failure and hypertensive disease.² It has both protective or detrimental effects in various tissues, including the heart, kidney, and vasculature.^3,1 Cayman’s Cardiotrophin-1 (human, recombinant) protein is a disulfide-linked homodimer. The reduced monomer, composed of cardiotrophin-1 (amino acids 2-201) fused to human IgG1 at its N-terminus, consists of 460 amino acids and has a calculated molecular weight of 49.5 kDa. As a result of glycosylation, the monomer migrates at approximately 54 kDa by SDS-PAGE under reducing conditions.

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