Mouse GDF-6/BMP-13 Antibody
Mouse GDF-6/BMP-13 Antibody Summary
Thr335-Arg454
Accession # P43028
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Applications
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.
Scientific Data
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GDF‑6/BMP‑13 in Mouse Embryo. GDF-6/BMP-13 was detected in immersion fixed frozen sections of mouse embryo (E13.5) using Sheep Anti-Mouse GDF-6/ BMP-13 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF855) at 10 µg/mL overnight at 4 °C. Tissue was stained using the NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (red; Catalog # NL010) and counterstained with DAPI (blue). Specific staining was localized to dorsal neural tube. View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections.
Reconstitution Calculator
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.
Background: GDF-6/BMP-13
Growth Differentiation Factor 6 (GDF-6), also known as bone morphogenetic protein 13 (BMP-13) or cartilage-derived morphogenetic protein 2 (CDMP-2), is a member of the bone morphogenetic protein (BMP) family which belongs to the transforming growth factor beta (TGF-beta ) superfamily. The mature GDF-6 with 120 amino acids is a homodimeric protein containing the characteristic seven conserved cysteine residues. GDF-5, GDF-6 and GDF-7, which share 80‑86% identity, define a new subgroup within the BMP family. Like other TGF-beta superfamily proteins, GDF-6 is highly conserved across species. At the amino acid sequence level, human and mouse GDF‑6 are 99% identical. It has been reported that GDF-6 has multiple functions including regulation of myogenesis, regulation of chondrogenesis, bone morphogenesis, and neuron differentiation and survival. GDF-6 response is mediated by the formation of hetero-oligomeric complexes of type I (BMPR-IB) and type II (BMPR-II or Activin R-II) sereine/threonine kinase receptors, and the activation of Smad proteins (Smad 1, 5, and 8).
- Storm, E.E. et al. (1994) Nature 368:639.
- Nishitoh, H. et al. (1996) J. Biol. Chem. 271:21345.
- Francis-West, P.H. et al. (1999) Development 126:1035.
- Massague, J. et al. (2000) Genes and Dev. 14:627.
- Inada, M. et al. (1996) BBRC, 222:317.
- Settle, S.H., Jr. et al. (2003) Dev. Biol. 254:116.
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