Recombinant Human/Mouse/Rat GDF-11/BMP-11 Protein

(11 citations)   

The Highest Quality, Most Active GDF-11 on the Market


Features and Benefits
  • Custom Quantities Available: Bulk amounts to meet your research needs. Please contact us.
  • High Purity: Determined by SDS-PAGE (>95%) and mass spectrometry.
  • Industry Low Endotoxin Specification: <0.1 EU/μg of protein greatly diminishes potential non-specific effects.
  • Lot-to-Lot Consistency: Stringent testing and analysis to ensure the same activity in future experiments.

  • Purity
    >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
  • Endotoxin Level
    <0.01 EU per 1 μg of the protein by the LAL method.
  • Activity
    Measured by its ability to induce hemoglobin expression in K562 human chronic myelogenous leukemia cells. Schwall, R.H. et al. (1991) Method Enzymol. 198:340. The ED50 for this effect is 0.8-4.8 ng/mL.
  • Source
    E. coli-derived Asn299-Ser407, with an N-terminal Met
  • Accession #
  • N-terminal Sequence
    Analysis
    Met-Asn299-Leu-Gly-Leu-Asp-(Cys)-Asp-Glu-His
  • Structure / Form
    Disulfide-linked homodimer
  • Predicted Molecular Mass
    12.6 kDa (monomer)
Carrier Free
What does CF mean?
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.
What formulation is right for me?
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.
1958-GD
 
1958-GD/CF
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin.
Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Data Images

Recombinant Human/Mouse/Rat
GDF‑11/BMP‑11 (Catalog # 1958-GD) induces hemoglobin expression in the K562 human chronic myelogenous leukemia cell line. The ED50 for this effect is 0.8-4.8 ng/mL.

1 μg/lane of Recombinant Human/Mouse/Rat GDF‑11/BMP-11 was resolved with
SDS-PAGE under reducing (R) and
non-reducing (NR) conditions and visualized by silver staining, showing bands at 13 kDa and 21 kDa, respectively.

Mass Spectrometry

ESI analysis of Recombinant Human/Mouse/Rat GDF-11/BMP-11. The peak at 25163 Da corresponds to the calculated molecular mass of the disulfide-linked homodimer.

Background: GDF-11/BMP-11
Growth Differentiation Factor 11 (GDF-11), also known as BMP-11, is a member of the TGF-beta superfamily and is highly related to GDF-8. GDF-11 encodes a 407 amino acid (aa) prepropeptide which contains a signal sequence for secretion and an RXXR proteolytic processing site to yield a 109 aa residue carboxy-terminal mature protein (1). Mature GDF-11 contains the canonical 7-cysteine motif common to other TGF-beta superfamily members; however, like the TGF-beta s, Activins and GDF-8, GDF-11 also contains one extra pair of cysteine residues. At the amino acid sequence level, mature human, mouse, rat and chicken GDF-11 are 99-100% identical. GDF-11 and GDF-8 share 90% amino acid sequence identity within the mature protein. As detected by in situ hybridization, GDF-11 is expressed in diverse regions of the mouse embryo: tailbud, somitic precursors, limbs, mandibular and branchial arches, dorsal neural tube, odontoblasts, nasal epithelium, and particular regions of the brain (1, 2). Targeted deletion of GDF-11, in mice, results in a spectrum of abnormalities including palatal malformation, vertebral defects, elongated trunks with a reduced or absent tail, missing or malformed kidneys, and an increased number of neurons in the olfactory epithelium (2-5). GDF-11 signals through the Activin type II receptors and induces phosphorylation of Smad2 to mediate axial patterning (6). Systemic GDF-11 levels decline with age and administration of higher levels of GDF-11 can reverse age-related cardiac hypertrophy (7). In addition, systemic administration of recombinant GDF-11 protein restores genomic integrity and health of muscle stem cells, neurovasculature and enhances neurogenesis (8, 9). R&D Systems recombinant GDF-11 preparations have been shown to act similarly to GDF-8 in both the Xenopus animal cap and the K562 assays.
  • References:
    1. Gamer, L.W. et al. (1999) Dev. Biol. 208: 222. 
    2. Nakashima, M. et al. (1999) Mech. Dev. 80:185.  
    3. Gad, J.M. and P.P.L. Tam (1999) Curr. Biol. 9:R783.  
    4. McPherron, A.C. et al. (1999) Nat. Genet. 22:260.
    5. Esquela, A.F. and S.J. Lee (2003) Dev. Biol. 257:356.
    6. Oh, S.P. et al. (2002) Genes & Dev. 16:274.
    7. Loffredo, F.S. et. al. (2013) Cell. 153.828.
    8. Katsimpardi, L. et. al. (2014) Science (ahead of print).
    9. Sinha, M. et. al. (2014) Science (ahead of print).
  • Long Name:
    Growth Differentiation Factor 11
  • Entrez Gene IDs:
    10220 (Human)
  • Alternate Names:
    BMP-11; BMP-11BMP11Bone morphogenetic protein 11; GDF11; GDF-11; growth differentiation factor 11; growth/differentiation factor 11
Related Research Areas
Citations:

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.

11 Citations: Showing 1 - 10
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Species
Applications
Sample Type
  1. Structural basis for potency differences between GDF8 and GDF11
    Authors: RG Walker, M Czepnik, EJ Goebel, JC McCoy, A Vujic, M Cho, J Oh, S Aykul, KL Walton, G Schang, DJ Bernard, AP Hinck, CA Harrison, E Martinez-H, AJ Wagers, RT Lee, TB Thompson
    BMC Biol, 2017;15(1):19.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  2. Maltose binding protein-fusion enhances the bioactivity of truncated forms of pig myostatin propeptide produced in E. coli
    Authors: SB Lee, SK Park, YS Kim
    PLoS ONE, 2017;12(4):e0174956.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  3. Supraphysiological levels of GDF11 induce striated muscle atrophy
    Authors: DW Hammers, M Merscham-B, JY Hsiao, S Engst, JJ Hartman, HL Sweeney
    EMBO Mol Med, 2017;0(0):.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  4. GDF11 does not improve the palmitate induced insulin resistance in C2C12
    Authors: YY Jing, D Li, F Wu, LL Gong, R Li
    Eur Rev Med Pharmacol Sci, 2017;21(8):1795-1802.
    Species: Mouse
    Sample Type: Whole Cells
    Application: Bioassay
  5. Activin A more prominently regulates muscle mass in primates than does GDF8
    Authors: E Latres, J Mastaitis, W Fury, L Miloscio, J Trejos, J Pangilinan, H Okamoto, K Cavino, E Na, A Papatheodo, T Willer, Y Bai, J Hae Kim, A Rafique, S Jaspers, T Stitt, AJ Murphy, GD Yancopoulo, J Gromada
    Nat Commun, 2017;8(0):15153.
    Species: Human
    Sample Type: Recombinant Protein
    Application: Surface Plasmon Resonance
  6. Specific targeting of TGF-? family ligands demonstrates distinct roles in the regulation of muscle mass in health and disease
    Authors: JL Chen, KL Walton, A Hagg, TD Colgan, K Johnson, H Qian, P Gregorevic, CA Harrison
    Proc. Natl. Acad. Sci. U.S.A., 2017;0(0):.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  7. Myostatin blockade with a fully human monoclonal antibody induces muscle hypertrophy and reverses muscle atrophy in young and aged mice.
    Authors: Latres E, Pangilinan J, Miloscio L, Bauerlein R, Na E, Potocky T, Huang Y, Eckersdorff M, Rafique A, Mastaitis J, Lin C, Murphy A, Yancopoulos G, Gromada J, Stitt T
    Skelet Muscle, 2015;5(0):34.
  8. An activin receptor IIA ligand trap promotes erythropoiesis resulting in a rapid induction of red blood cells and haemoglobin.
    Authors: Carrancio S, Markovics J, Wong P, Leisten J, Castiglioni P, Groza M, Raymon H, Heise C, Daniel T, Chopra R, Sung V
    Br J Haematol, 2014;165(6):870-82.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  9. An activin receptor IIA ligand trap corrects ineffective erythropoiesis in beta-thalassemia.
    Authors: Dussiot M, Maciel T, Fricot A, Chartier C, Negre O, Veiga J, Grapton D, Paubelle E, Payen E, Beuzard Y, Leboulch P, Ribeil J, Arlet J, Cote F, Courtois G, Ginzburg Y, Daniel T, Chopra R, Sung V, Hermine O, Moura I
    Nat Med, 2014;20(4):398-407.
    Species: Mouse
    Sample Type: Whole Cells
    Application: Bioassay
  10. Soluble Endoglin Specifically Binds Bone Morphogenetic Proteins 9 and 10 via Its Orphan Domain, Inhibits Blood Vessel Formation, and Suppresses Tumor Growth.
    Authors: Castonguay R, Werner ED, Matthews RG, Presman E, Mulivor AW, Solban N, Sako D, Pearsall RS, Underwood KW, Seehra J, Kumar R, Grinberg AV
    J. Biol. Chem., 2011;286(34):30034-46.
    Species: Human
    Sample Type: Recombinant Protein
    Application: Surface Plasmon Resonance
  11. TGFbeta ligands promote the initiation of retinal ganglion cell dendrites in vitro and in vivo.
    Authors: Hocking JC, Hehr CL, Chang RY, Johnston J, McFarlane S
    Mol. Cell. Neurosci., 2007;37(2):247-60.
    Species: Xenopus
    Sample Type: Whole Cells
    Application: Bioassay
Expand to show all 11 Citations

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