Mouse GDF-3 Biotinylated Antibody
Mouse GDF-3 Biotinylated Antibody Summary
Accession # Q07104
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Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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, adipose tissue and the brain (2-4). In ES cells, it maintains pluripotency and influences early cell fate decisions (5, 6). For example, frog embryos injected with GDF-3 develop a secondary dorsal axis and deletion of mouse GDF-3 can produce defects in the anterior visceral endoderm of the pre‑gastrulation embryo (5, 6). In adipocytes, GDF-3 is induced by a high fat diet and promotes adipogenesis (3). GDF-3 has been reported to oppose BMP’s functions and to have a nodal-like activity in early development (1). 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. Most of GDF-3 is present as the prepro form, while the mature GDF-3 is presumably the secreted, active form (1). The mature protein contains the cysteine-knot structure that is conserved throughout family members. Since it lacks the fourth cysteine, which is responsible for the formation of inter-molecular disulfide bond, GDF-3 may exist as a non-covalent homodimer. Mature mouse GDF-3 shares 90%, 83%, and 83% aa identity with rat, human and canine GDF-3, respectively. Among family members, mature GDF-3 is most similar to mouse BMP-6 (45% aa identity) and Xenopus VG‑1 (52% aa identity).
- 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.
- Wang, W. et al. (2004) Biochem. Biophys. Res. Comm. 321:1024.
- Hexige, S. et al. (2005) Neurosci. Lett. 389:83.
- Levine, A.J. and A.H. Brivanlou (2005) Development 133:209.
- Chen, C. et al. (2006) Development 133:319.
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