Human BMP-9 Propeptide Antibody

Catalog # Availability Size / Price Qty
AF3879
AF3879-SP
Product Details
Citations (5)
FAQs
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Human BMP-9 Propeptide Antibody Summary

Species Reactivity
Human
Specificity
Detects human BMP-9 Propeptide in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with mature recombinant human BMP-9 is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Chinese hamster ovary cell line CHO-derived recombinant human BMP‑9 Propeptide
Lys23-Arg319
Accession # Q9UK05
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.

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human BMP‑9 Propeptide

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

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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: BMP-9

Human BMP-9, also known as growth and differentiation factor 2 (GDF-2), is a member of the BMP subgroup of the TGF-beta superfamily proteins that signal through heterodimeric complexes composed of type I and type II BMP receptors. BMP-9 regulates the development and function of a variety of embryonal and adult tissues (1, 2). The human BMP-9 cDNA encodes a 429 amino acid (aa) precursor that includes a 22 aa signal sequence, a 298 aa propeptide, and a 111 aa mature protein (3). Unlike with other BMP family proteins, the propeptide does not interfere with the biological activity of BMP-9 and remains associated with the mature peptide after proteolytic cleavage (4). Human and mouse BMP-9 share 96% aa sequence identity. Within the mature protein, human BMP-9 shares 64% aa sequence identity with human BMP-10 and less than 50% aa sequence identity with other BMPs. BMP-9 is expressed by non-parenchymal cells in the liver, (5, 6) where it promotes lipid metabolism and inhibits glucose production (7). BMP-9 exerts a prolonged hypoglycemic effect which may be due to an enhancement of insulin release (7). BMP-9 interacts with a high affinity specific heteromeric receptor expressed on liver endothelial cells that has been identified as ALK-1 (4‑6). In the embryonal CNS, BMP-9 functions in the development and maintenance of the cholinergic neuronal phenotype (8‑10). BMP-9 also induces the differentiation of mesenchymal stem cells into the chondrogenic lineage (11, 12). At low concentrations, BMP-9 is a proliferative factor for hematopoietic progenitor cells, but at higher concentrations, it enhances TGF-beta 1 production and inhibits hematopoietic progenitor colony formation (13).

References
  1. Chen, D. et al. (2004) Growth Factors 22:233.
  2. Miyazono, K. et al. (2005) Cytokine Growth Factor Rev. 16:251.
  3. Celeste, A.J. et al. (1994) J. Bone Miner. Res. 9:S136.
  4. Brown, M.A. et al. (2005) J. Biol. Chem. 280:25111.
  5. Song, J.J. et al. (1995) Endocrinology 136:4293.
  6. Miller, A.F. et al. (2000) J. Biol. Chem. 275:17937.
  7. Chen, C. et al. (2003) Nat. Biotechnol. 21:294.
  8. Lopez-Coviella, I. et al. (2000) Science 289:313.
  9. Lopez-Coviella, I. et al. (2005) Proc. Natl. Acad. Sci. 102:6984.
  10. Lopez-Coviella, I. et al. (2002) J. Physiol. Paris 96:53.
  11. Majumdar, M.K. et al. (2001) J. Cell. Physiol. 189:275.
  12. Hills, R.L. et al. (2005) J. Orthoped. Res. 23:611.
  13. Ploemacher, R.E. et al. (1999) Leukemia 13:428.
Long Name
Bone Morphogenetic Protein 9
Entrez Gene IDs
2658 (Human); 12165 (Mouse)
Alternate Names
BMP9; BMP-9; BMP9BMP-9Bone morphogenetic protein 9; GDF2; GDF-2; growth differentiation factor 2; growth/differentiation factor 2

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Citations for Human BMP-9 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.

5 Citations: Showing 1 - 5
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  1. Bone Morphogenetic Protein 9 Reduces Cardiac Fibrosis and Improves Cardiac Function in Heart Failure
    Authors: Kevin J. Morine, Xiaoying Qiao, Sam York, Peter S. Natov, Vikram Paruchuri, Yali Zhang et al.
    Circulation
  2. Preferential Induction of the T Cell Auxiliary Signaling Molecule B7-H3 on Synovial Monocytes in Rheumatoid Arthritis
    Authors: BR Yoon, YH Chung, SJ Yoo, K Kawara, J Kim, IS Yoo, CG Park, SW Kang, WW Lee
    J. Biol. Chem, 2015-12-23;291(8):4048-57.
    Species: Human
    Sample Types: Protein
    Applications: ELISA Development (Capture)
  3. Rapid Activation of Bone Morphogenic Protein 9 by Receptor-mediated Displacement of Pro-domains
    Authors: Y Kienast, U Jucknischk, S Scheiblich, M Thier, M de Wouters, A Haas, C Lehmann, V Brand, D Bernicke, K Honold, S Lorenz
    J. Biol. Chem, 2015-12-16;291(7):3395-410.
    Species: Human
    Sample Types: Protein
    Applications: ELISA Development (Capture)
  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
  5. Regulation of Bone Morphogenetic Protein 9 (BMP9) by Redox-dependent Proteolysis*
    Authors: Zhenquan Wei, Richard M. Salmon, Paul D. Upton, Nicholas W. Morrell, Wei Li
    Journal of Biological Chemistry

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