Detects human GDF-3 in direct ELISAs.
In direct ELISAs, no cross-reactivity
with recombinant human (rh) GDF-1, rhBMP-2, or rhBMP-6 is observed and
approximately 5% cross-reactivity with recombinant mouse GDF-3 homodimer is
Monoclonal Mouse IgG1 Clone # 741614
Protein A or G purified from hybridoma culture supernatant
Chinese hamster ovary cell line CHO-derived recombinant human GDF-3 Ala251-Gly364 Accession # Q9NR23
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
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.
GDF‑3 in BG01V Human Embryonic Stem Cells. GDF‑3 was detected in immersion fixed BG01V human embryonic stem cells using Mouse Anti-Human GDF‑3 Monoclonal Antibody (Catalog # MAB5754) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
Preparation and Storage
Sterile PBS to a final concentration of 0.5 mg/mL.
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.
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 364 amino acid (aa) human GDF-3 contains a 21 aa signal sequence, a 229 aa propeptide and a 114 aa mature region 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%, 91%, 92% and 93% aa identity with mouse, rat, bovine, canine and equine 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 human ES cells, inhibition of BMP-2 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 (ALK-1, -2, -3 and -6), which activate Smads 1, 5 and 8, GDF-3 signaling through ALK-4 and ALK-7, 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).
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