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Mouse GDF-8/Myostatin Propeptide Antibody

Catalog #: AF1539
11 Citations Datasheet / COA / SDS
Catalog # Availability Size / Price Qty
AF1539
AF1539-SP
GDF‑8 Propeptide Inhibition of GDF‑8/Myostatin-induced Hemoglobin Expression and Neutralization by Mouse GDF‑8 Propeptide Antibody.
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Citations (11)
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Mouse GDF-8/Myostatin Propeptide Antibody Summary

Species Reactivity
Mouse
Specificity
Detects GDF‑8/Myostatin Propeptide in direct ELISAs and Western blots. In direct ELISAs, less than 10% cross‑reactivity with mature recombinant mouse (rm) GDF-8 is observed and less than 5% cross-reactivity with mature rmGDF-1, -3, -5, -6, -7, -9, and recombinant human GDF-11 is observed.
Source
Polyclonal Sheep IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse GDF‑8/Myostatin Propeptide
Asn25-Ser265
Accession # O08689
Formulation
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.
Endotoxin Level
<0.10 EU per 1 μg of the antibody by the LAL method.

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Mouse GDF‑8/Myostatin Propeptide (Catalog # 1539-PG)
Neutralization
Measured by its ability to neutralize GDF‑8 Propeptide inhibition of GDF‑8/Myostatin-dependent hemoglobin expression in the K562 human chronic myelogenous leukemia cell line. The Neutralization Dose (ND50) is typically 10-30 µg/mL in the presence of 800 ng/mL Recombinant Mouse GDF‑8 Propeptide and 40 ng/mL Recombinant Mouse GDF‑8/Myostatin.

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

Neutralization GDF‑8 Propeptide Inhibition of GDF‑8/Myostatin-induced Hemoglobin Expression and Neutralization by Mouse GDF‑8 Propeptide Antibody. View Larger

GDF‑8 Propeptide Inhibition of GDF‑8/Myostatin-induced Hemoglobin Expression and Neutralization by Mouse GDF‑8 Propeptide Antibody. Recombinant Mouse GDF-8 Propeptide (Catalog # 1539-PG) inhibits Recombinant Mouse GDF-8/Myostatin (Catalog # 788-G8) induced hemoglobin expression in the K562 human chronic myelogenous leukemia cell line in a dose-dependent manner (orange line), as measured by the psuedoperoxidase assay. Inhibition of Recombinant Mouse GDF-8/Myostatin (40 ng/mL) activity elicited by Recombinant Mouse GDF-8 Propeptide (800 ng/mL) is neutralized (green line) by increasing concentrations of Sheep Anti-Mouse GDF-8/Myostatin Propeptide Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1539). The ND50 is typically 10-30 µg/mL.

Western Blot Detection of Mouse GDF-8/Myostatin by Western Blot View Larger

Detection of Mouse GDF-8/Myostatin by Western Blot Myostatin precursors redistribute during atrophy. (a) Western blot using a polyclonal antibody raised to the prodomain of myostatin. Recombinant protein controls (proMyostatin and latent myostatin) are used to visualize the migration of proMyostatin and myostatin prodomain bands. In muscle from a pilot experiment in which mice were administered dexamethasone for 15 days, proMyostatin levels increase in muscle, while the levels of latent myostatin in plasma (inferred from the prodomain band) decrease. (b) In a follow-on experiment, animals were administered either vehicle (No Dex) or dexamethasone in their drinking water for two weeks, and given a single 20 mg/kg dose of test antibodies (SRK-015 or IgG control) at day 1. Differences in gastrocnemius muscle weights (expressed as percent difference from the mean of the IgG (no Dex) control group) are shown for days 4, 6, 8 and 15. Individual data points (n = 8–10 animals) along with means +/− standard deviations are shown. Group means were compared by one-way ANOVA followed by a Holm-Sidak test. (c–e) Quantitation of proMyostatin and latent myostatin levels in murine muscle and serum at 4, 6, 8, and 15 days following either dexamethasone or vehicle administration. For all data presented, a minimum of three biological replicates were measured to generate the presented average values, and error bars on all graphs represent standard deviations. Statistical significance was determined by t test (two-tailed, homoscedastic). Image collected and cropped by CiteAb from the following publication (https://www.nature.com/articles/s41598-018-20524-9), licensed under a CC-BY license. Not internally tested by R&D Systems.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store 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.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: GDF-8/Myostatin

Growth Differentiation Factor 8 (GDF-8), also known as Myostatin, is a secreted TGF-beta superfamily protein that is expressed specifically in developing and adult skeletal muscle. It controls myoblast proliferation and is a potent negative regulator of skeletal muscle mass (1‑3). Mouse GDF-8 is synthesized as a 376 amino acid (aa) preproprotein that consists of a 24 aa signal peptide, a 243 aa propeptide, and a 109 aa mature protein (2). Within the propeptide, mouse GDF-8 shares 96% and 99% aa sequence identity with human and rat GDF-8, respectively. GDF-8 is secreted as a preproprotein that is cleaved by BMP-1 family proteases to separate the 35‑40 kDa propeptide from the 12 kDa bioactive mature protein (4‑6). This results in a latent complex containing a disulfide-linked dimer of the mature protein and two noncovalently-associated molecules of the propeptide (2, 6). The GDF-8 propeptide functions as an inhibitor of mature GDF-8, and GDF-8 activity can also be inhibited through association with Follistatin, FLRG, Decorin, or GASP-1 (6‑11). The uncleaved GDF-8 proprotein binds Latent TGF-beta bp3 which can sequester it in the extracellular matrix and prevent the proteolytic cleavage of the propeptide (12). GDF-8 binds to the type II Activin receptor Activin RIIB which then associates with the type I receptors Activin RIB/ALK-4 or TGF-beta RI/ALK-5 to induce signaling (13). GDF-8 additionally inhibits adipogenic differentiation of mesenchymal stem cells and preadipocytes (14). Genetic deletion of GDF-8 or in vivo administration of the GDF-8 propeptide induces muscle hypertrophy as well as enhanced glucose utilization and insulin sensitivity and a reduction in overall fat mass (15, 16).

References
  1. McPherron, A.C. (2010) Immunol. Endocr. Metab. Agents Med. Chem. 10:217.
  2. McPherron, A.C. et al. (1997) Nature 387:83.
  3. Zimmers, T.A. et al. (2002) Science 296:1486.
  4. Wolfman, N.M. et al. (2003) Proc. Natl. Acad. Sci. 100:15842.
  5. McFarlane, C. et al. (2005) Dev. Biol. 283:58.
  6. Lee, S.J. et al. (2001) Proc. Natl. Acad. Sci. 98:9306.
  7. Thies, R.S. et al. (2001) Growth Factors 18:251.
  8. Amthor, H. et al. (2004) Dev. Biol. 270:19.
  9. Hill, J.J. et al. (2002) J. Biol. Chem. 277:40735.
  10. Miura, T. et al. (2006) Biochem. Biophys. Res. Commun. 340:675.
  11. Hill, J.J. et al. (2003) Molecular Endocrinology 17:1144.
  12. Anderson, S.B. et al. (2008) J. Biol. Chem. 283:7027.
  13. Rebbapragada, A. et al. (2003) Mol. Cell. Biol. 23:7230.
  14. Guo, W. et al. (2008) J. Biol. Chem. 283:9136.
  15. Matsakas, A. et al. (2009) Neuromuscul. Disord. 19:489.
  16. Guo, T. et al. (2009) PloS ONE 4:e4937.
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; MSLHP; MSTN; Myostatin

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Citations for Mouse GDF-8/Myostatin Propeptide 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.

11 Citations: Showing 1 - 10
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  1. Latent myostatin has significant activity and this activity is controlled more efficiently by WFIKKN 1 than by WFIKKN 2
    Authors: György Szláma, Mária Trexler, László Patthy
    The FEBS Journal
  2. Myostatin Is Upregulated Following Stress in an Erk-Dependent Manner and Negatively Regulates Cardiomyocyte Growth in Culture and in a Mouse Model
    Authors: Lawrence T. Bish, Kevin J. Morine, Meg M. Sleeper, H. Lee Sweeney
    PLoS ONE
  3. Myostatin: a Circulating Biomarker Correlating with Disease in Myotubular Myopathy Mice and Patients
    Authors: C Koch, S Buono, A Menuet, A Robé, S Djeddi, C Kretz, R Gomez-Oca, M Depla, A Monseur, L Thielemans, L Servais, J Laporte, BS Cowling
    Mol Ther Methods Clin Dev, 2020-05-04;17(0):1178-1189.
    Species: Mouse, Transgenic Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  4. Blocking extracellular activation of myostatin as a strategy for treating muscle wasting
    Authors: M Pirruccell, J Jackson, S Wawersik, MT Webster, L Salta, K Long, W McConaughy, A Capili, C Boston, GJ Carven, NK Mahanthapp, KJ Turner, A Donovan
    Sci Rep, 2018-02-02;8(1):2292.
    Species: Mouse
    Sample Types: Tissue Homogenates
    Applications: Western Blot
  5. The Use of Platelet-Rich and Platelet-Poor Plasma to Enhance Differentiation of Skeletal Myoblasts: Implications for the Use of Autologous Blood Products for Muscle Regeneration
    Authors: O Miroshnych, WT Chang, JL Dragoo
    Am J Sports Med, 2016-12-27;45(4):945-953.
    Species: Human
    Sample Types: Platelet Rich Plasma (PRP)
    Applications: Immunoprecipitation
  6. 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, 2015-10-09;5(0):34.
    Species: Human, Mouse
    Sample Types: Cell Culture Supernates, Serum
    Applications: Western Blot
  7. A satellite cell-specific knockout of the androgen receptor reveals myostatin as a direct androgen target in skeletal muscle.
    Authors: Dubois V, Laurent M, Sinnesael M, Cielen N, Helsen C, Clinckemalie L, Spans L, Gayan-Ramirez G, Deldicque L, Hespel P, Carmeliet G, Vanderschueren D, Claessens F
    FASEB J, 2014-03-26;28(7):2979-94.
    Species: Mouse
    Sample Types: Tissue Homogenates
    Applications: Western Blot
  8. Myostatin expression, lymphocyte population, and potential cytokine production correlate with predisposition to high-fat diet induced obesity in mice.
    Authors: Lyons JA, Haring JS, Biga PR
    PLoS ONE, 2010-09-22;5(9):e12928.
    Species: Mouse
    Sample Types: Tissue Homogenates
    Applications: Western Blot
  9. 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., 2008-03-13;283(20):13874-88.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Western Blot
  10. 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., 2006-10-12;116(11):2924-34.
    Species: Mouse
    Sample Types: Tissue Homogenates
    Applications: Immunoprecipitation
  11. K153R polymorphism in myostatin gene increases the rate of promyostatin activation by furin
    Authors: György Szláma, Mária Trexler, László Buday, László Patthy
    FEBS Letters

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