Recombinant Mouse GDF-9 Protein, CF

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Recombinant Mouse GDF-9 induces Mv1Lu mink lung epithelial cell death. The ED50 for this effect is 0.1-0.4 μg/mL.

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse 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 0.1-0.4 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse GDF-9 protein
Gly307-Arg441
Accession #
N-terminal Sequence
Gly307
Protein/Peptide Type
Recombinant Proteins
Gene
Gdf9
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
15.6 kDa.
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.
SDS-PAGE
20 kDa, reducing conditions
Publications
Read Publications using
739-G9/CF in the following applications:

Packaging, Storage & Formulations

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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in HCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in 4 mM HCl.

Notes

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

Alternate Names for Recombinant Mouse GDF-9 Protein, CF

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

Background

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 mouse GDF-9 has a predicted molecular weight of 15.6 kDa, and shares 90% and 95% amino acid sequence identity with mature human and rat GDF-9, respectively. It forms both non-covalent homodimers and heterodimers with BMP-15, which is coordinately expressed with GDF-9 in the oocyte. (3-5). 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 (9, 10). It is critical for the growth of granulosa and theca cells and for the differentiation and maturation of the oocyte (11, 12). GDF-9 is thought to act synergistically with BMP-15 to control development of the oocyte-cumulus cell complex (5, 12-14). In mice, GDF-9:BMP-15 heterodimers have been shown to be more potent regulators of granulosa cell functions compared to GDF-9 homodimers (6). Studies on GDF-9 null mice have demonstrated arrested follicular development at the primary follicle stage (10). In humans, aberrant GDF-9 expression and activation is associated with a multitude of common human ovarian disorders including premature ovarian failure and polycystic ovary syndrome (15-17).
  1. McPherron, A.C. and S.J. Lee (1993) J. Biol. Chem. 268:3444.
  2. McGrath, S. A. et al. (1995) Mol. Endocrinol. 9:131.
  3. Laitinen, M. et al. (1998) Mech. Dev. 78:135.
  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. Elvin, J.A. et al. (1999) Mol. Endocrinol. 13:1035.
  10. Dong, J. et al. (1996) Nature 383:531.
  11. Hreinsson, J.G. et al. (2002) J. Clin. Endocrinol. Metab. 87:316.
  12. Su, Y.Q. et al. (2004) Dev. Biol. 276:64.
  13. Yan, C. et al. (2001) Mol. Endocrinol. 15:854.
  14. Mottershead, D.G. et al. (2012) Mol. Hum. Reprod. 18:121.
  15. Zhao, S.Y. et al. (2010) Fertil. Steril. 94:261.
  16. Wei, L.N. et al. (2011) Fertil. Steril. 96:464.
  17. Simpson, C.M. et al. (2014) J. Clin. Endocrinol. Metab. [Epub ahead of print].

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Publications for GDF-9 (739-G9/CF)(8)

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 3 applications: Bioassay, Western Blot, Western Blot Control.


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Bioassay
(6)
Western Blot
(1)
Western Blot Control
(1)
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Human
(1)
Mouse
(7)
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Showing Publications 1 - 8 of 8.
Publications using 739-G9/CF Applications Species
K Komatsu, S Masubuchi Mouse oocytes connect with granulosa cells by fusing with cell membranes and form a large complex during follicle development Biol. Reprod., 2018;0(0):. 2018 [PMID: 29590310] (Western Blot Control, Mouse) Western Blot Control Mouse
S El-Hayek, Q Yang, L Abbassi, G FitzHarris, HJ Clarke Mammalian Oocytes Locally Remodel Follicular Architecture to Provide the Foundation for Germline-Soma Communication Curr. Biol., 2018;0(0):. 2018 [PMID: 29576478] (Bioassay, Mouse) Bioassay Mouse
N Kong, X Xu, Y Zhang, Y Wang, X Hao, Y Zhao, J Qiao, G Xia, M Zhang Natriuretic peptide type C induces sperm attraction for fertilization in mouse Sci Rep, 2017;7(0):39711. 2017 [PMID: 28054671] (Bioassay, Mouse) Bioassay Mouse
Oocyte-dependent activation of MTOR in cumulus cells controls the development and survival of cumulus-oocyte complexes J Cell Sci, 2016;0(0):. 2016 [PMID: 27358481] (Bioassay, Mouse) Bioassay Mouse
Mottershead D, Sugimura S, Al-Musawi S, Li J, Richani D, White M, Martin G, Trotta A, Ritter L, Shi J, Mueller T, Harrison C, Gilchrist R Cumulin, an Oocyte-secreted Heterodimer of the Transforming Growth Factor-beta Family, Is a Potent Activator of Granulosa Cells and Improves Oocyte Quality. J Biol Chem, 2015;290(39):24007-20. 2015 [PMID: 26254468] (Western Blot, Human) Western Blot Human
Sudiman J, Sutton-McDowall M, Ritter L, White M, Mottershead D, Thompson J, Gilchrist R Bone morphogenetic protein 15 in the pro-mature complex form enhances bovine oocyte developmental competence. PLoS ONE, 2014;9(7):e103563. 2014 [PMID: 25058588] (Bioassay, Mouse) Bioassay Mouse
Mottershead D, Ritter L, Gilchrist R Signalling pathways mediating specific synergistic interactions between GDF9 and BMP15. Mol Hum Reprod, 2012;18(3):121-8. 2012 [PMID: 21911477] (Bioassay, Mouse) Bioassay Mouse
Sugiura K, Su YQ, Li Q, Wigglesworth K, Matzuk MM, Eppig JJ Fibroblast growth factors and epidermal growth factor cooperate with oocyte-derived members of the TGFbeta superfamily to regulate Spry2 mRNA levels in mouse cumulus cells. Biol. Reprod., 2009;81(5):833-41. 2009 [PMID: 19553596] (Bioassay, Mouse) Bioassay Mouse

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Bioinformatics

Gene Symbol Gdf9
Uniprot