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Recombinant Mouse GDF-3 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Mouse GDF-3 Protein, CF Summary

Details of Functionality
Measured by its ability to bind with Recombinant Human Activin RIB/ALK‑4 Fc Chimera (Catalog # 808-AR) in the presence of Recombinant Mouse Cripto (Catalog # 1538-CR) in functional ELISA. Chen, et al. (2006) Development 133:319. Immobilized Recombinant Mouse (rm) GDF-3 at 1 µg/mL (100 µL/well) can bind Recombinant Human Activin RIB/ALK‑4 Fc Chimera (Catalog # 808-AR) with an apparent Kd <100 nM.
The activity of rmGDF-3 is not fully tested in cell-based assays. Please contact Technical Service for product related questions.
Source
E. coli-derived mouse GDF-3 protein
Ala253-Gly366
Accession #
N-terminal Sequence
Ala253
Protein/Peptide Type
Recombinant Proteins
Gene
Gdf3
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
13.1 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.

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 Acetonitrile and TFA.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCI.

Notes

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

Alternate Names for Recombinant Mouse GDF-3 Protein, CF

  • GDF3
  • GDF-3
  • growth differentiation factor 3
  • growth/differentiation factor 3
  • KFS3
  • MCOP7
  • MCOPCB6
  • Vgr-2

Background

GDF-3 (previously called Vgr-2) is a TGF-beta superfamily member belonging to the growth/differentiation factor family (1, 2). GDF-3 is expressed in undifferentiated embryonic stem (ES) cells, white adipose tissue and the brain (2-4). The 366 amino acid (aa) mouse GDF-3 contains a 22 aa signal sequence, a 230 aa propeptide and a 114 aa mature protein that contains one potential N-glycosylation site. The mature region contains a cysteine-knot structure that is conserved throughout family members. However, it lacks the fourth cysteine which is responsible for the formation of an inter-molecular disulfide bond, so GDF-3 may exist as a non-covalent homodimer (2, 5). Mature mouse GDF-3 shares 90% and 83% aa sequence identity with rat and human GDF-3, respectively. Most of GDF-3 is present as the uncleaved prepro form (6). The uncleaved and the mature forms both appear to have activity, but that activity may differ (5-8). All forms can oppose BMPs. In ES cells, inhibition of BMP2 signaling by GDF-3 maintains pluripotency (5, 7). GDF-3 also influences early cell fate decisions; for example, deletion of mouse GDF-3 produces defects in the anterior visceral endoderm of the pre-gastrulation embryo (6-8). GDF-3 cooperates with GDF-1 in embryogenesis, and the mature protein has nodal-like activity (8, 9). Although GDF family members signal through BMP receptors (ALK1, 2, 3 and 6), which activate Smads 1, 5 and 8, GDF-3 signaling through ALK4 and ALK7, which activate Smads 2 and 3, has also been reported (9, 10). In adipocytes, GDF-3 is induced by a high fat diet, promoting adipogenesis and obesity (3, 10, 11).
  1. Levine, A.J. and A.H. Brivanlou (2006) Cell Cycle 5:1069.
  2. McPherron, A.C. and S.-J. Lee (1993) J. Biol. Chem. 268:3444. Mouse cloning
  3. Wang, W. et al. (2004) Biochem. Biophys. Res. Comm. 321:1024.
  4. Hexige, S. et al. (2005) Neurosci. Lett. 389:83.
  5. Levine, A.J. et al. (2009) Dev. Biol. 325:43.
  6. Levine, A.J. and A.H. Brivanlou (2005) Development 133:209.
  7. Peerani, R. et al. (2007) EMBO J. 26:4744.
  8. Chen, C. et al. (2006) Development 133:319.
  9. Andersson, O. et al. (2007) Dev. Biol. 311:500.
  10. Andersson, O. et al. (2008) Proc. Natl. Acad. Sci. USA 105:7252.
  11. Shen, J.J. et al. (2009) Mol. Endocrinol. 23:113.

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Bioinformatics

Gene Symbol Gdf3
Uniprot