|Detection of Rat BMP‑15/GDF‑9B by Western Blot. Western blot shows lysates of rat ovary tissue. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Mouse/Rat BMP‑15/GDF‑9B Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5917) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for BMP‑15/GDF‑9B proprecursor at approximately 54 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
BMP-15 (Bone morphogenetic protein 15; also GDF-9B) is a 24-26 kDa member of the TGF-beta superfamily of proteins. It is expressed by late primary follicle oocytes, where it promotes the transition of preantral granulosa cells to cumulus cells, and later the expansion of cumulus cells. Mouse BMP-15 proprecursor is a 50-55 kDa, 367 amino acid (aa) glycoprotein. It is proteolytically cleaved to generate a 40 kDa prosegment (aa 26-267) plus a 24 kDa, 124 aa mature region (aa 268-392) that may be phosphorylated (on Ser7 of the mature molecule) and/or glycosylated. Secreted BMP-15 does not occur as a mature homodimer, but it does exist as a mature monomer, an uncleaved proprecursor, or as a noncovalent heterodimer composed of a cleaved mature region and its prosegment. The heterodimer may also form an oligomer. The BMP-15 prosegment reportedly forms a noncovalent heterodimer with 20 kDa mature GDF-9. Mature mouse BMP-15 shares 70% and 91% aa identity with human and rat BMP-15, respectively.
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