Home / BMP-10 / Human BMP-10 Propeptide Biotinylated Antibody

Human BMP-10 Propeptide Biotinylated Antibody

Catalog #: BAF3956
4 Citations Datasheet / COA / SDS
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BAF3956
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Citations (4)
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Human BMP-10 Propeptide Biotinylated Antibody Summary

Species Reactivity
Human
Specificity
Detects human BMP-10 Propeptide in Western blots. In Western blots, less than 1% cross-reactivity with mature recombinant human BMP-10 is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human BMP-10 Propeptide
Ser20-Arg313
Accession # O95393
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human BMP‑10 Propeptide (Catalog # 3956-BP)

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.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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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.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: BMP-10

BMP-10, along with BMP-9, GDF-5, -6, and -7, belongs to a subgroup of sequence related TGF-beta superfamily proteins that signal through heterodimeric complexes composed of type I and type II BMP receptors (1‑3). Proteolytic removal of the propeptide from the 60 kDa proprotein yields a 12 kDa mature BMP-10 which forms disulfide-linked non-glycosylated homodimers (4, 5). In transfectants, BMP-10 is secreted as a cleaved mature dimer, an uncleaved proform dimer, and an uncleaved proform monomer (4). The propeptide of human BMP-10 shares 82% amino acid sequence identity with mouse and rat proBMP-10 and 19%‑34% with the propeptides of human BMP-9, GDF-5, -6, and -7. BMP-10 is critical for the proper development of the heart and first appears at the onset of trabeculation and chamber formation (6‑8). Homozygous BMP-10 knockout mice die in utero due to arrested cardiac development (7). BMP-10 is required for maintaining expression of the cardiogenic transcription factors NKX2.5 and MEF2C in developing myocardium and promoting the growth of embryonic cardiomyocytes (7, 9, 10). The BMP-10 mediated proliferation of these cells requires Notch signaling (11). NKX2.5 itself negatively regulates BMP-10 expression in cardiac myocytes (10). Multiple human congenital heart defects result from mutations in NKX2.5 and require BMP-10 expression (10). In mice, genetic knockout of ErbB leads to a similar phenotype but appears not to involve BMP-10, and knockout of the calcium channel subunit FKBP12 induces BMP-10 overexpression (7). BMP-10 in the postnatal heart promotes increased cardiomyocyte and heart size (8). BMP-10 has been shown to induce signaling through ALK-1, BMPR-IA, BMPR-IB, and BMPR-II in transfectants and non-cardiac cell lines (4, 5). A functional BMP-10 receptor in the heart has not yet been identified, although deletion of BMPR-IA or BMP-10 causes similar cardiac morphogenetic abnormalities (12).

References
  1. Chen, D. et al. (2004) Growth Factors 22:233. 
  2. Miyazono, K. et al. (2005) Cytokine Growth Factor Rev. 16:251. 
  3. Schneider, M.D. et al. (2003) Cytokine Growth Factor Rev. 14:1. 
  4. Mazerbourg, S. et al. (2005) J. Biol. Chem. 280:32122. 
  5. David, L. et al. (2007) Blood 109:1953. 
  6. Neuhaus, H. et al. (1999) Mech. Dev. 80:181. 
  7. Chen, H. et al. (2004) Development 131:2219.
  8. Chen, H. et al. (2006) J. Biol. Chem. 281:27481.
  9. Srivastava, D. and E.N. Olson (2000) Nature 407:221.
  10. Pashmforoush, M. et al. (2004) Cell 117:373.
  11. Grego-Bessa, J. et al. (2007) Dev. Cell 12:415.
  12. Gaussin, V. et al. (2002) Proc. Natl. Acad. Sci. 99:2878.
Long Name
Bone Morphogenetic Protein 10
Entrez Gene IDs
27302 (Human); 12154 (Mouse)
Alternate Names
BMP10; BMP-10; bone morphogenetic protein 10; MGC126783

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Citations for Human BMP-10 Propeptide Biotinylated 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.

4 Citations: Showing 1 - 4
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  1. Crystal structures of BMPRII extracellular domain in binary and ternary receptor complexes with BMP10
    Authors: J Guo, B Liu, M Thorikay, M Yu, X Li, Z Tong, RM Salmon, RJ Read, P Ten Dijke, NW Morrell, W Li
    Nature Communications, 2022-05-03;13(1):2395.
    Species: Human
    Sample Types: Recombinant Proteins
    Applications: ELISA Detection
  2. Reduced circulating BMP10 and BMP9 and elevated endoglin are associated with disease severity, decompensation and pulmonary vascular syndromes in patients with cirrhosis
    Authors: NE Owen, GJ Alexander, S Sen, K Bunclark, G Polwarth, J Pepke-Zaba, AP Davenport, NW Morrell, PD Upton
    EBioMedicine, 2020-05-23;56(0):102794.
    Species: Human
    Sample Types: Plasma
    Applications: ELISA (detection)
  3. The Prodomain-bound Form of Bone Morphogenetic Protein 10 Is Biologically Active on Endothelial Cells*
    Authors: He Jiang, Richard M. Salmon, Paul D. Upton, Zhenquan Wei, Aleksandra Lawera, Anthony P. Davenport et al.
    Journal of Biological Chemistry
  4. Homozygous GDF2 nonsense mutations result in a loss of circulating BMP9 and BMP10 and are associated with either PAH or an “HHT‐like” syndrome in children
    Authors: Joshua Hodgson, Lidia Ruiz‐Llorente, Jamie McDonald, Oliver Quarrell, Kelechi Ugonna, James Bentham et al.
    Molecular Genetics & Genomic Medicine

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