Formulation: Lyophilized from sterile PBS, pH 7.4.
Purity: ≥92% estimated by SDS-PAGE
Formula Weight: 0
Shelf life (days): 365
Notes: Growth differentiation factor 8 (GDF8) is a myokine and member of the TGF-β superfamily.{68920,68921} It is produced in skeletal and cardiac muscle cells as a proprotein, which shares sequence identity between the human, mouse, and rat.{68920,68924} The proprotein is cleaved in the endoplasmic reticulum into a protein containing a prodomain and C-terminal signaling domain.{68920,68922,68924} This protein is secreted and forms homodimers that either circulate or remain near the extracellular membrane in a latent state.{68925} The prodomain is cleaved by bone morphogenetic protein 1 (BMP1) or tolloid family metalloproteinases, releasing the signaling domain to activate TGF-β receptor type 2 (TGFBR2) and negatively regulate muscle growth and differentiation.{68925,68920,68921} 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.{68923} The levels of full-length GDF8 and GDF8 prodomain are increased in left ventricle tissue samples from patients with dilated- or ischemic cardiomyopathy.{68924} 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.
Deutsch
English
