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 K d <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 |
|
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
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).
- Levine, A.J. and A.H. Brivanlou (2006) Cell Cycle 5:1069.
- McPherron, A.C. and S.-J. Lee (1993) J. Biol. Chem. 268:3444. Mouse cloning
- Wang, W. et al. (2004) Biochem. Biophys. Res. Comm. 321:1024.
- Hexige, S. et al. (2005) Neurosci. Lett. 389:83.
- Levine, A.J. et al. (2009) Dev. Biol. 325:43.
- Levine, A.J. and A.H. Brivanlou (2005) Development 133:209.
- Peerani, R. et al. (2007) EMBO J. 26:4744.
- Chen, C. et al. (2006) Development 133:319.
- Andersson, O. et al. (2007) Dev. Biol. 311:500.
- Andersson, O. et al. (2008) Proc. Natl. Acad. Sci. USA 105:7252.
- Shen, J.J. et al. (2009) Mol. Endocrinol. 23:113.
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