Activin B, Mouse ELISA

Activins, like all members of the transforming growth factor-beta superfamily, are synthesized as large pro-hormones with N-terminal pro- and C-terminal mature domains. Studies have shown that the prodomains template the dimerization of pro-activin forms, that are subsequently processed to yield pro/mature fragments. The prodomains, although important for folding and extracellular localization, must be removed prior to activity. Activin forms retaining the prodomain are biologically inactive.

Activin B, like certain other members of the TGF-β family, signals through the ActRII receptor (Activin Receptor type II). Human Activin B is a 25.6 kDa disulfide-linked homodimer consisting of two βB chains, each containing 115 amino acid residues.

Activin B exhibits a wide range of biological activities, including regulation of embryogenesis, osteogenesis, hematopoiesis, reproductive physiology and hormone secretion from the hypothalamic, pituitary and gonadal glands.