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Recombinant Mouse GDF-9 Protein

Catalog #: 739-G9
15 Citations 1 Review Datasheet / COA / SDS

Carrier Free

Catalog # Availability Size / Price Qty
739-G9-010/CF

With Carrier

Catalog # Availability Size / Price Qty
739-G9-010
Recombinant Mouse GDF-9 Protein Bioactivity
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Product Details
Citations (15)
FAQs
Reviews (1)
Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Mouse GDF-9 Protein Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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 #
AAA53035
N-terminal Sequence
Analysis
Gly307
Predicted Molecular Mass
15.6 kDa
SDS-PAGE
20 kDa, reducing conditions

Product Datasheets

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739-G9 (with carrier)

Product Datasheet
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SDS

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739-G9/CF (carrier free)

Product Datasheet
COA
SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

739-G9

Formulation Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in 4 mM HCl containing 0.1% bovine serum albumin.
Shipping 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

739-G9/CF

Formulation Lyophilized from a 0.2 μm filtered solution in HCl.
Reconstitution Reconstitute at 100 μg/mL in 4 mM HCl.
Shipping 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Scientific Data

Bioactivity Recombinant Mouse GDF-9 Protein Bioactivity View Larger

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

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: GDF-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 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).

References
  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].
Long Name
Growth Differentiation Factor 9
Entrez Gene IDs
2661 (Human); 14566 (Mouse)
Alternate Names
GDF9; GDF-9; growth differentiation factor 9; growth/differentiation factor 9

Citations for Recombinant Mouse GDF-9 Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

15 Citations: Showing 1 - 10
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  1. Novel Insight into the mechanism of di (2-ethylhexyl) phthalate (DEHP) impairing early follicle development
    Authors: Feng, M;Wang, J;Zhao, X;Du, H;Dai, Y;
    Ecotoxicology and environmental safety
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: Bioassay
  2. Generation of functional oocytes from male mice in vitro
    Authors: K Murakami, N Hamazaki, N Hamada, G Nagamatsu, I Okamoto, H Ohta, Y Nosaka, Y Ishikura, TS Kitajima, Y Semba, Y Kunisaki, F Arai, K Akashi, M Saitou, K Kato, K Hayashi
    Nature, 2023-03-15;615(7954):900-906.
    Species: Mouse
    Sample Types: Transfected Whole Cells
    Applications: Bioassay
  3. Cooperative effects of oocytes and estrogen on the forkhead box L2 expression in mural granulosa cells in mice
    Authors: H Ito, C Emori, M Kobayashi, N Maruyama, W Fujii, K Naito, K Sugiura
    Scientific Reports, 2022-11-23;12(1):20158.
    Species: Mouse
    Sample Types:
    Applications: Bioassay
  4. Offspring production of ovarian organoids derived from spermatogonial stem cells by defined factors with chromatin reorganization
    Authors: H Luo, X Li, GG Tian, D Li, C Hou, X Ding, L Hou, Q Lyu, Y Yang, AJ Cooney, W Xie, J Xiong, H Wang, X Zhao, J Wu
    Journal of advanced research, 2021-03-17;33(0):81-98.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Activation-induced cytidine deaminase is a possible regulator of cross-talk between oocytes and granulosa cells through GDF-9 and SCF feedback system
    Authors: T Iizuka, K Wakae, M Ono, T Suzuki, Y Mizumoto, K Kitamura, SI Horike, M Muramatsu, H Fujiwara
    Scientific Reports, 2021-02-15;11(1):3833.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Reconstitution of the oocyte transcriptional network with transcription factors
    Authors: N Hamazaki, H Kyogoku, H Araki, F Miura, C Horikawa, N Hamada, S Shimamoto, O Hikabe, K Nakashima, TS Kitajima, T Ito, HG Leitch, K Hayashi
    Nature, 2020-12-16;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Cell Culture
  7. Cyclooxygenase 2 messenger RNA levels in canine follicular cells: interrelationship with GDF-9, BMP-15, and progesterone
    Authors: M De Los Rey, J Palomino, A Araujo, J Flores, G Ramirez, VH Parraguez, K Aspee
    Domest. Anim. Endocrinol., 2020-08-06;74(0):106529.
    Species: Canine
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Mouse oocytes connect with granulosa cells by fusing with cell membranes and form a large complex during follicle development
    Authors: K Komatsu, S Masubuchi
    Biol. Reprod., 2018-09-01;0(0):.
    Species: Mouse
    Sample Types: Recombinant Protein
    Applications: Western Blot Control
  9. Mammalian Oocytes Locally Remodel Follicular Architecture to Provide the Foundation for Germline-Soma Communication
    Authors: S El-Hayek, Q Yang, L Abbassi, G FitzHarris, HJ Clarke
    Curr. Biol., 2018-03-22;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  10. Natriuretic peptide type C induces sperm attraction for fertilization in mouse
    Authors: N Kong, X Xu, Y Zhang, Y Wang, X Hao, Y Zhao, J Qiao, G Xia, M Zhang
    Sci Rep, 2017-01-05;7(0):39711.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Oocyte-dependent activation of MTOR in cumulus cells controls the development and survival of cumulus-oocyte complexes
    J Cell Sci, 2016-06-29;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  12. Cumulin, an Oocyte-secreted Heterodimer of the Transforming Growth Factor-beta Family, Is a Potent Activator of Granulosa Cells and Improves Oocyte Quality.
    Authors: 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
    J Biol Chem, 2015-08-08;290(39):24007-20.
    Species: Human
    Sample Types: Protein
    Applications: Western Blot
  13. Bone morphogenetic protein 15 in the pro-mature complex form enhances bovine oocyte developmental competence.
    Authors: Sudiman J, Sutton-McDowall M, Ritter L, White M, Mottershead D, Thompson J, Gilchrist R
    PLoS ONE, 2014-07-24;9(7):e103563.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  14. Signalling pathways mediating specific synergistic interactions between GDF9 and BMP15.
    Authors: Mottershead D, Ritter L, Gilchrist R
    Mol Hum Reprod, 2011-09-12;18(3):121-8.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  15. 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.
    Authors: Sugiura K, Su YQ, Li Q, Wigglesworth K, Matzuk MM, Eppig JJ
    Biol. Reprod., 2009-06-24;81(5):833-41.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay

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Recombinant Mouse GDF-9 Protein
By Anonymous on 10/09/2020
Application: CellProlif