Recombinant Human GDF-9 Protein, CF


1 μg/lane of Recombinant Human GDF-9 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing single bands at 20 kDa and 26 kDa, respectively.
Recombinant Human GDF-9 (Catalog # 8266-G9/CF) induces Mv1Lu mink lung epithelial cell death. The ED50 for this effect is 50-250 ng/mL.

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Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human GDF-9 Protein, CF Summary

Details of Functionality
Measured by its ability to induce cell death using Mv1Lu mink lung epithelial cells. The ED50 for this effect is 50-250 ng/mL.
Human embryonic kidney cell, HEK293-derived human GDF-9 protein
Gly320-Arg454 (Gly391Arg)
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


Theoretical MW
16 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
20-22 kDa, reducing conditions

Packaging, Storage & Formulations

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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in HCl.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCl.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human GDF-9 Protein, CF

  • GDF9
  • GDF-9
  • growth differentiation factor 9
  • growth/differentiation factor 9


Growth Differentiation Factor-9 (GDF-9) is an oocyte secreted paracrine factor in the TGF-beta superfamily (1, 2). It is synthesized as a prepropeptide and is subsequently processed by proteases into the mature protein (1, 2). Mature human GDF-9 has a predicted molecular weight of 16 kDa and shares 89.6% and 91.9% amino acid sequence identity with the mouse and rat orthologs, respectively. Despite the high homology, mouse GDF-9 is secreted in an active form, while human GDF-9 is latent. A single mutation Gly391Arg increases the affinity between human GDF-9 and its signaling receptors and make it more active (3). It forms both non-covalent homodimers and heterodimers with BMP-15, which is coordinately expressed with GDF-9 in the oocyte. (2, 4, 5). GDF-9 signals through TGF-beta RI/ALK-5 and BMPR-II, while the GDF-9:BMP-15 heterodimer is believed to signal through BMPR-II, ALK 4/5/7, and BMPR-IB/ALK-6 (5-8). SMAD2 and SMAD3 are phosphorylated following activation of receptor complexes by GDF-9 (5, 6). GDF-9 functions as a paracrine factor in the development of primary follicles in the ovary. It is critical for the growth of granulosa and theca cells and for the differentiation and maturation of the oocyte (5, 9-11). GDF-9 is thought to act synergistically with BMP-15 to control development of the oocyte-cumulus cell complex (4-6). In humans, GDF-9:BMP-15 heterodimers have been shown to be more potent regulators of granulosa cell functions compared to GDF-9 homodimers (6). Aberrant GDF-9 expression and activation is associated with a multitude of common human ovarian disorders including premature ovarian failure and polycystic ovary syndrome (10, 12-14). In breast and bladder cancers, GDF-9 is believed to function as a tumor suppressor because its expression levels are inversely correlated with the aggressiveness of the cancer (15, 16). In prostate cancer, however, GDF-9 may enhance tumor progression by promoting tumor cell growth and epithelial-to-mesenchymal transition (17, 18).

  1. McGrath, S. A. et al. (1995) Mol. Endocrinol. 9:131.
  2. Aaltonen, J. et al. (1999) J. Clin. Endocrinol. Metab. 84:2744.
  3. Simpson, C.M. et al. (2012) 153:1301.
  4. Liao, W.X. et al. (2003) J. Biol. Chem. 278:3713.
  5. Gilchrist, R.B. et al. (2008) Hum. Reprod. Update 14:159.
  6. Peng, J. et al. (2013) Proc. Natl. Acad. Sci. USA 110:E776.
  7. Vitt, U.A. et al. (2002) Biol. Reprod. 67:473.
  8. Mazerbourg, S. et al. (2004) Mol. Endocrinol. 18:653.
  9. Hreinsson, J.G. et al. (2002) J. Clin. Endocrinol. Metab. 87:316.
  10. Otsuka, F. et al. (2011) Mol. Reprod. Dev. 78:9.
  11. Dong, J. et al. (1996) Nature 383:531.
  12. Zhao, S.Y. et al. (2010) Fertil. Steril. 94:261.
  13. Wei, L.N. et al. (2011) Fertil. Steril. 96:464.
  14. Simpson, C.M. et al. (2014) J. Clin. Endocrinol. Metab. [Epub ahead of print].
  15. Hanavadi, S. et al. (2007) Ann. Surg. Oncol. 14:2159.
  16. Du, P. et al. (2012) Int. J. Mol. Med. 29:428.
  17. Bokobza, S.M. et al. (2010) J. Cell. Physiol. 225:529.
  18. Bokobza, S.M. et al. (2011) Mol. Cell. Biochem. 349:33.

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Gene Symbol GDF9