Detects human, mouse, and rat GDF‑8/Myostatin in Western blots. In Western blots, approximately 15% cross-reactivity with recombinant human/mouse/rat GDF-11 is observed, 10% cross-reactivity with recombinant mouse (rm) GDF‑3 is observed, and less than 2% cross-reactivity with rmGDF-1, rmGDF-5, and rmGDF-6 is observed.
Polyclonal Goat IgG
E. coli-derived recombinant mouse GDF‑8/Myostatin Asp268-Ser376 Accession # O08689
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
GDF‑8/Myostatin was detected in immersion fixed frozen sections of mouse embryo (lung) using Goat Anti-Human/Mouse/Rat GDF‑8/Myostatin Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF788) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Growth Differentiation Factor 8 (GDF-8), also known as myostatin, is a member of the TGF-beta superfamily that is expressed specifically in developing and adult skeletal muscle. GDF-8 cDNA encodes a 376 amino acid (aa) prepropeptide with a 24 aa residue signal peptide, a 223 aa residue amino-terminal propeptide, and a 109 aa residue carboxy-terminal mature protein. Mature GDF-8 contains the canonical 7-cysteine motif common to other TGF-beta superfamily members. Similar to the TGF‑ beta s, activins and BMP-11, GDF-8 also contains one extra pair of cysteine residues that is not found in other family members. The bioactive form of GDF-8 is a homodimer with an apparent molecular weight of approximately 25 kDa. GDF-8 is highly conserved across species. At the amino acid sequence level, mature human, mouse, rat and cow GDF-8 are 100% identical. Within the TGF-beta superfamily, GDF-8 is most closely related to BMP-11, a mammalian protein that acts as a dorsal mesoderm and neural inducer in Xenopus explants. The two proteins share 90% amino acid sequence identity within their mature chain. A targeted disruption of GDF-8 in mouse results in large mice with a widespread increase in skeletal muscle mass, indicating that GDF-8 is a negative regulator of skeletal muscle growth. A mutation in the bovine GDF-8 gene has been shown to be responsible for the double-muscled phenotype in cattle breeds such as Belgian Blue cattle that is characterized by an increase in muscle mass. GDF‑8 has also been shown to inhibit preadipocyte differentiation to adipocytes. Mature GDF-8 binds to activin type II receptors and the binding is antagonized by the activin-binding protein, follistatin. R&D Systems recombinant GDF-8 preparations have been shown to act similarly to Activin A in both the Xenopus animal cap and the K562 assays.
Storm, E.E. et al. (1994) Nature 368:639
Sharma, M. et al. (1999) J. Cell Physiol. 180:1
McPherron, A.C. et al. (1997) Nature 387:83
Lee, S.J. et al. (2001) Proc. Natl. Acad. Sci. USA 98:9306
Kim, H.S. et al. (2001) Biochem. Biophys. Res. Commun. 281:902
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