Mouse GDF-9 Propeptide Antibody
Mouse GDF-9 Propeptide Antibody Summary
Accession # AAA53035
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Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 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-9 (GDF-9) is a member of the transforming growth factor-beta (TGF-beta ) superfamily, and is an oocyte secreted paracrine factor essential for mammalian ovarian folliculogenesis (1‑2). Mouse GDF-9 is synthesized as a 441 amino acid (aa) prepropeptide that contains a 29 aa signal sequence, a 277 aa propeptide, and a 135 aa mature chain. Residues 340‑441 constitute a TGF-beta like domain. In addition, there is one potential site of N-linked glycosylation in the mature chain. Unlike other members of the TGF-beta superfamily, GDF-9 lacks the conserved cysteine residue that is believed to form the sole disulfide linkage between subunits in other family members (3). Mature mouse GDF-9 shares 90% aa sequence identity with mature human GDF 9. The protein is expressed throughout the development of the maturing follicle (2). GDF-9 functions as a paracrine factor in the regulation of granulosa cell proliferation and differentiation, and is essential for fertility (2, 4). Studies on GDF-9 null mice have demonstrated arrested follicular development at the primary follicle stage (5). Mouse GDF-9 induces Smad2 phosphorylation and inhibin production in rat diethylstilbestrol treated granulosa cells (6) and in human granulosa-luteal cells (7). The downstream signaling actions of GDF 9 are mediated by the type I receptor, activin receptor-like kinase 5 (ALK5), initiating the subsequent activation of Smad2 and Smad3 (2, 8). GDF 9 uses the BMP type II receptor (BMPRII) as its other signaling receptor (2, 9).
- McGrath, S.A. et al. (1995) Mol. Endocrinol. 9:131.
- Mottershead, D.G. et al. (2008) Mol. Cell. Endocrinol. 283:58.
- McPherron, A.C. and S.-J. Lee (1992) J. Biol. Chem. 268:3444.
- Gilchrist, R.B. et al. (2006) J. Cell. Sci. 119:3811.
- Dong, J. et al. (1996) Nature 383:531.
- Roh, J.S. et al. (2003) Endocrinology 144:172.
- Kaivo-Oja, N. et al. (2003) J. Clin. Endocrinol. Metab. 88:755.
- Mazerbourg, S. et al. (2004) Mol. Endocrinol. 18:653.
- Vitt, U.A. et al. (2002) Biol. Reprod. 67:473.
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