Recombinant Mouse GDF-3 Protein Summary
Product Specifications
Ala253-Gly366
Analysis
Product Datasheets
Carrier Free
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.
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.
9009-GD
| 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 |
| 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.
|
9009-GD/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 with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Scientific Data
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Recombinant Mouse GDF-3 (Catalog # 9009-GD) Induces Smad2 phosphorylation in P19 mouse embryonic carcinoma cells. P19 cells were incubated with 50 and 100 ng/ml of Recombinant Mouse GDF-3 for 60 minutes. The cells were lysed and Western blots were performed with anti-phospho Smad2 and eIF4E which was served as a loading control.
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1 μg/lane of Recombinant Mouse GDF-3 (Catalog # 9009-GD) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing R bands at 16 and 17 kDa and NR bands at 16 and 18 kDa.
Reconstitution Calculator
Background: GDF-3
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). GDF3 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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