Recombinant Human/Mouse/Rat GDF-8/Myostatin Protein, CF

  (24 citations)     
Datasheet / CoA / SDS
Product Details
Citations (24)
FAQs
Reviews
  • Purity
    >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
  • Endotoxin Level
    <0.10 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 2-10 ng/mL.
  • Source
    Mouse myeloma cell line, NS0-derived GDF-8/Myostatin protein
    Asp268-Ser376
  • Accession #
  • N-terminal Sequence
    Analysis
    Asp268
  • Structure / Form
    Disulfide-linked homodimer
  • Predicted Molecular Mass
    12.4 kDa
  • SDS-PAGE
    12 kDa, reducing conditions
    24 kDa, non-reducing conditions
Product Datasheets

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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.
788-G8/CF
 
788-G8
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
 
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl.
 
Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin.
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-8/
Myostatin (Catalog # 788-G8/CF) induces hemoglobin expression in the K562 human chronic myelogenous leukemia cell line. The ED50 for this effect is 2-10 ng/mL.
1 μg/lane of Recombinant Human/Mouse/Rat GDF-8/Myostatin was resolved with
SDS-PAGE under reducing (R) and
non-reducing (NR) conditions and visualized by silver staining, showing the main bands at 12 kDa and 24 kDa, respectively.
Background: GDF-8/Myostatin

Growth Differentiation Factor 8 (GDF-8), also known as myostatin, is a member of the TGF-beta superfamily that is expressed specifically in developing and adult skeletal muscle. GDF-8 cDNA encodes a 376 amino acid (aa) prepropeptide with a 24 aa residue signal peptide, a 223 aa residue amino-terminal propeptide, and a 109 aa residue carboxy-terminal mature protein. Mature GDF-8 contains the canonical 7-cysteine motif common to other TGF-beta superfamily members. Similar to the TGF‑ beta s, activins and BMP-11, GDF-8 also contains one extra pair of cysteine residues that is not found in other family members. The bioactive form of GDF-8 is a homodimer with an apparent molecular weight of approximately 25 kDa. GDF-8 is highly conserved across species. At the amino acid sequence level, mature human, mouse, rat and cow GDF-8 are 100% identical. Within the TGF-beta superfamily, GDF-8 is most closely related to BMP-11, a mammalian protein that acts as a dorsal mesoderm and neural inducer in Xenopus explants. The two proteins share 90% amino acid sequence identity within their mature chain. A targeted disruption of GDF-8 in mouse results in large mice with a widespread increase in skeletal muscle mass, indicating that GDF-8 is a negative regulator of skeletal muscle growth. A mutation in the bovine GDF-8 gene has been shown to be responsible for the double-muscled phenotype in cattle breeds such as Belgian Blue cattle that is characterized by an increase in muscle mass. GDF-8 has also been shown to inhibit preadipocyte differentiation to adipocytes. Mature GDF-8 binds to activin type II receptors and the binding is antagonized by the activin-binding protein, follistatin. R&D Systems recombinant GDF-8 preparations have been shown to act similarly to Activin A in both the Xenopus animal cap and the K562 assays.

  • References:
    1. Storm, E.E. et al. (1994) Nature 368:639.
    2. Sharma, M. et al. (1999) J. Cell Physiol. 180:1.
    3. McPherron, A.C. et al. (1997) Nature 387:83.
    4. Lee, S.J. et al. (2001) Proc. Natl. Acad. Sci. USA 98:9306.
    5. Kim, H.S. et al. (2001) Biochem. Biophys. Res. Commun. 281:902.
  • Long Name:
    Growth Differentiation Factor 8
  • Entrez Gene IDs:
    2660 (Human); 17700 (Mouse)
  • Alternate Names:
    GDF8; GDF-8; GDF8growth differentiation factor 8; growth/differentiation factor 8; MSTN; Myostatin
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.

24 Citations: Showing 1 - 10
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Species
Applications
Sample Type
  1. Relative abundance of mature myostatin rather than total myostatin is negatively associated with bone mineral density in Chinese
    Authors: LF Wu, DC Zhu, BH Wang, YH Lu, P He, YH Zhang, HQ Gao, XW Zhu, W Xia, H Zhu, XB Mo, X Lu, L Zhang, YH Zhang, FY Deng, SF Lei
    J. Cell. Mol. Med., 2017;0(0):.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  2. The histone deacetylase SIRT6 blocks myostatin expression and development of muscle atrophy
    Authors: SA Samant, A Kanwal, VB Pillai, R Bao, MP Gupta
    Sci Rep, 2017;7(1):11877.
    Species: Mouse
    Sample Type: Whole Cells
    Application: Bioassay
  3. 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
  4. 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
  5. 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
  6. 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
  7. 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
  8. Myostatin propeptide mutation of the hypermuscular Compact mice decreases the formation of myostatin and improves insulin sensitivity
    Authors: Tamas Kocsis
    Am. J. Physiol. Endocrinol. Metab, 2016;0(0):ajpendo.00216.
    Application: positive control
  9. 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.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  10. Small molecules dorsomorphin and LDN-193189 inhibit myostatin/GDF8 signaling and promote functional myoblast differentiation.
    Authors: Horbelt D, Boergermann J, Chaikuad A, Alfano I, Williams E, Lukonin I, Timmel T, Bullock A, Knaus P
    J Biol Chem, 2015;290(6):3390-404.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  11. A Key Role for Leukemia Inhibitory Factor in C26 Cancer Cachexia.
    Authors: Seto D, Kandarian S, Jackman R
    J Biol Chem, 2015;290(32):19976-86.
    Species: Mouse
    Sample Type: Whole Cells
    Application: Bioassay
  12. Blockade of ActRIIB signaling triggers muscle fatigability and metabolic myopathy.
    Authors: Relizani K, Mouisel E, Giannesini B, Hourde C, Patel K, Morales Gonzalez S, Julich K, Vignaud A, Pietri-Rouxel F, Fortin D, Garcia L, Blot S, Ritvos O, Bendahan D, Ferry A, Ventura-Clapier R, Schuelke M, Amthor H
    Mol Ther, 2014;22(8):1423-33.
    Species: Mouse
    Sample Type: Whole Cells
    Application: Bioassay
  13. Screening with a novel cell-based assay for TAZ activators identifies a compound that enhances myogenesis in C2C12 cells and facilitates muscle repair in a muscle injury model.
    Authors: Yang, Zeyu, Nakagawa, Kentaro, Sarkar, Aradhan, Maruyama, Junichi, Iwasa, Hiroaki, Bao, Yijun, Ishigami-Yuasa, Mari, Ito, Shigeru, Kagechika, Hiroyuki, Hata, Shoji, Nishina, Hiroshi, Abe, Shinya, Kitagawa, Masanobu, Hata, Yutaka
    Mol Cell Biol, 2014;34(9):1607-21.
    Species: Mouse
    Sample Type: Whole Cells
    Application: Bioassay
  14. Myostatin regulates energy homeostasis in the heart and prevents heart failure.
    Authors: Biesemann N, Mendler L, Wietelmann A, Hermann S, Schafers M, Kruger M, Boettger T, Borchardt T, Braun T
    Circ Res, 2014;115(2):296-310.
    Species: Mouse
    Sample Type: Whole Cells
    Application: Bioassay
  15. Myostatin stimulates, not inihibits, C2C12 myoblast proliferation.
    Authors: Rodgers B, Wiedeback B, Hoversten K, Jackson M, Walker R, Thompson T
    Endocrinology, 2014;155(3):670-5.
    Species: Mouse
    Sample Type: Whole Cells
    Application: Bioassay
  16. Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors.
    Authors: Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J
    Nature, 2012;487(7408):505-9.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  17. Self-renewal of embryonic-stem-cell-derived progenitors by organ-matched mesenchyme.
    Authors: Sneddon, Julie B, Borowiak, Malgorza, Melton, Douglas
    Nature, 2012;491(7426):765-8.
    Species: Human
    Sample Type: Whole Cells
    Application: Cell Culture Substrate
  18. Analysis of the effects of androgens and training on myostatin propeptide and follistatin concentrations in blood and skeletal muscle using highly sensitive Immuno PCR.
    Authors: Diel P, Schiffer T, Geisler S, Hertrampf T, Mosler S, Schulz S, Wintgens KF, Adler M
    Mol. Cell. Endocrinol., 2010;330(1):1-9.
    Species: N/A
    Sample Type: N/A
    Application: ELISA Standard
  19. Loss-of-function mutation in myostatin reduces tumor necrosis factor alpha production and protects liver against obesity-induced insulin resistance.
    Authors: Wilkes JJ, Lloyd DJ, Gekakis N
    Diabetes, 2009;58(5):1133-43.
    Species: Mouse
    Sample Type: In Vivo
    Application: In Vivo
  20. Targeting of bone morphogenetic protein growth factor complexes to fibrillin.
    Authors: Sengle G, Charbonneau NL, Ono RN, Sasaki T, Alvarez J, Keene DR, Bachinger HP, Sakai LY
    J. Biol. Chem., 2008;283(20):13874-88.
    Species: Human
    Sample Type: Recombinant Protein
    Application: complex formation
  21. A new model for growth factor activation: type II receptors compete with the prodomain for BMP-7.
    Authors: Sengle G, Ono RN, Lyons KM, Bachinger HP, Sakai LY
    J. Mol. Biol., 2008;381(4):1025-39.
    Species: Human
    Sample Type: Recombinant Protein
    Application: ELISA development
  22. Gene transfer demonstrates that muscle is not a primary target for non-cell-autonomous toxicity in familial amyotrophic lateral sclerosis.
    Authors: Miller TM, Kim SH, Yamanaka K, Hester M, Umapathi P, Arnson H, Rizo L, Mendell JR, Gage FH, Cleveland DW, Kaspar BK
    Proc. Natl. Acad. Sci. U.S.A., 2006;103(51):19546-51.
    Species: Mouse
    Sample Type: Whole Cells
    Application: Bioassay
  23. Muscular atrophy of caveolin-3-deficient mice is rescued by myostatin inhibition.
    Authors: Ohsawa Y, Hagiwara H, Nakatani M, Yasue A, Moriyama K, Murakami T, Tsuchida K, Noji S, Sunada Y
    J. Clin. Invest., 2006;116(11):2924-34.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  24. Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis.
    Authors: Amthor H, Nicholas G, McKinnell I, Kemp CF, Sharma M, Kambadur R, Patel K
    Dev. Biol., 2004;270(1):19-30.
    Species: Chicken
    Sample Type: Whole Tissue
    Application: Bioassay
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