Growth differentiation factor 8 (GDF8), or myostatin, is a member of the transforming growth factor-β superfamily that acts as a negative regulator of skeletal muscle growth and differentiation. This human latent GDF-8 protein is expressed from human 293 cells (HEK293) and contains amino acids Asn 24 to Ser 375 with an N-terminal His tag. The protein is designed as a dimer and is verified by mass spectrometry and SEC-MALS.
- Greater than 90% purity by SDS-PAGE and >95% purity by SEC-MALS.
- Low endotoxin levels, less than 0.01 EU per μg.
- Lyophilized from a 0.22 μm filtered solution of PBS, 0.2 M Arginine, pH 7.4 with trehalose.
- Achieves 98.7% sequence coverage in LC-MS/MS peptide mapping.
- Validated by binding activity assays for Activin RIIB, Follistatin, and Apitegromab.