Measured by its ability to induce Smad2 phosphorylation in P19 mouse embryonal carcinoma cells. Mazerbourg, S. et al. (2004) Mol. Endocrinol. 18:653. 50 ng/mL of Recombinant Human GDF-3 can effectively induce Smad2 phosphorylation.
Source
Chinese Hamster Ovary cell line, CHO-derived human GDF-3 protein Ala251-Gly364
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
12.9 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
18 kDa, reducing conditions
Publications
Read Publications using 5754-G3 in the following applications:
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 with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in 4 mM HCl containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human GDF-3 Protein
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 human GDF-3 shares 83%, 83% aa sequence identity with mouse and rat GDF-3. 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.
Caricasole, A.A. et al. (1998) Oncogene 16:95.
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.
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