GDF8 Signaling Domain (human, recombinant)

Growth differentiation factor 8 (GDF8) is a myokine and member of the TGF-beta superfamily.1,2 It is produced in skeletal and cardiac muscle cells as a proprotein, which shares sequence identity between the human, mouse, and rat.1,3 The proprotein is cleaved in the endoplasmic reticulum into a protein containing a prodomain and C-terminal signaling domain.1,4,3 This protein is secreted and forms homodimers that either circulate or remain near the extracellular membrane in a latent state.5 The prodomain is cleaved by bone morphogenetic protein 1 (BMP1) or tolloid family metalloproteinases, releasing the signaling domain to activate TGF-beta receptor type 2 (TGFBR2) and negatively regulate muscle growth and differentiation.5,1,2 Knockout of Myst, the gene expressing Gdf8, increases muscle mass, muscle fiber length, bone mineral content (BMC), and bone size in Myst-/- mice compared to wild-type mice.6 The levels of full-length GDF8 and GDF8 prodomain are increased in left ventricle tissue samples from patients with dilated- or ischemic cardiomyopathy.3 Cayman's GDF8 Signaling Domain (human, recombinant) protein is a disulfide-linked homodimer. The reduced monomer, composed of GDF8 (amino acids 267-375) fused to human IgG1 Fc at its N-terminus, consists of 369 amino acids and has a calculated molecular weight of 40.8 kDa. This protein consists of 108 amino acids and has a predicted N-terminus of Gly20 after signal peptide cleavage. As a result of glycosylation, the monomer migrates to approximately 45 kDa by SDS-PAGE under reducing conditions. WARNING This product is not for human or veterinary use. Purity: >92% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg determined by the LAL endotoxin assay. Source: Recombinant human N-terminal human IgG1 FC-tagged GDF8 signaling domain expressed in HEK293 cells. Amino Acids: 267-375. MW: 40.8 kDa. Formulation: Lyophilized from sterile PBS, pH 7.4.