Mouse GDF-3 Antibody

Catalog # Availability Size / Price Qty
Product Details
Citations (1)
Supplemental Products

Mouse GDF-3 Antibody Summary

Species Reactivity
Detects mouse GDF-3 in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross‑reactivity with recombinant mouse GDF-1, -5, -6, -7, -8, or -9 is observed.
Monoclonal Rat IgG2A Clone # 144728
Protein A or G purified from hybridoma culture supernatant
E. coli-derived recombinant mouse GDF-3
Accession # Q07104
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.


Recommended Concentration
Western Blot
1 µg/mL
Recombinant Mouse GDF‑3 (Catalog # 958-G3)

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.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & 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.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

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, 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).

  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.
  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. and A. H. Brivanlou (2005) Development 133:209.
  6. Chen, C. et al. (2006) Development 133:319.
Long Name
Growth Differentiation Factor 3
Entrez Gene IDs
9573 (Human); 14562 (Mouse)
Alternate Names
GDF3; GDF-3; growth differentiation factor 3; growth/differentiation factor 3; KFS3; MCOP7; MCOPCB6; Vgr-2

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Citation for Mouse GDF-3 Antibody

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. Obesity-Linked PPAR gamma S273 Phosphorylation Promotes Insulin Resistance through Growth Differentiation Factor 3
    Authors: Jessica A. Hall, Deepti Ramachandran, Hyun C. Roh, Joanna R. DiSpirito, Thiago Belchior, Peter-James H. Zushin et al.
    Cell Metabolism


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