Recombinant Human BMP-3 Protein, CF

Catalog # Availability Size / Price Qty
113-BP-100/CF
R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (4)
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Recombinant Human BMP-3 Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to inhibit BMP-2-induced activity in MC3T3‑E1 mouse preosteoblast cells. Daluiski, A. et al. (2001) Nature Genetics 27:84. 30 µg/mL of hBMP-3 will antagonize hBMP-2 (0.25 µg/mL) induction of alkaline phosphatase in MC3T3E1 cells by >50%.
Source
E. coli-derived human BMP-3 protein
Gln363-Arg472, with an N-terminal Met
Accession #
N-terminal Sequence
Analysis
Met
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
12.5 kDa (monomer)

Product Datasheets

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113-BP/CF (carrier free)

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.

113-BP/CF

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitution Reconstitute at 1 mg/mL in sterile 35% Acetonitrile and 0.1% TFA.
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.
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Background: BMP-3

BMP-3, also known as osteogenin, the most abundant BMP in adult bone, is one of at least 15 structurally and functionally related BMPs, which are members of the TGF-  beta superfamily (1 - 3). BMPs were originally identified as protein regulators of cartilage and bone formation. They have since been shown to be involved in embryogenesis and morphogenesis of various tissues and organs. BMPs also regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Similar to most other TGF-beta family proteins, BMPs are highly conserved across animal species. At the amino acid sequence level, mature human and rat BMP-3 are 98% identical. BMP-3 is synthesized as a large precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxy-terminal domain. Biologically active BMP-3 is a disulfide-linked homodimer of the carboxy-terminal 110 amino acid residues that contains the characteristic seven conserved cysteine residues involved in the formation of the cysteine knot and the single interchain disulfide bond (4). The role of BMP-3 in bone is contradictory since, unlike osteogenin purified from bone, recombinant BMP-3 has not shown osteogenic function (5). Several studies indicate that BMP-3 is an inhibitor of osteogenic BMPs. BMP-3 dorsalizes Xenopus embryos, the opposite effect of BMP-2 or 4, which cause ventralization. BMP-3 inhibits alkaline phosphatase production and induction of osteoblastic target genes in undifferentiated mesenchymal and osteogenic cell lines that have been treated with BMP-2. BMP-3 also induces the expression of TGF-beta /activin responsive genes, but not BMP-responsive genes. Since the inhibitory effect is not due to direct competition with osteogenic BMPs, it has been suggested that BMP-3 activates signaling through an activin pathway, resulting in antagonism of osteogenesis induced by other BMPs.

References
  1. Chen, D. et al. (2004) Growth Factors 22:233.
  2. Hino, J. et al. (2004) Front. Biosci. 9:1520.
  3. Bahamonde, M.E. and K.M. Lyons (2001) J. Bone and Joint Surgery 83-A (suppl 1):S156.
  4. Wozney, J.M. et al. (1998) Science 242:1528.
  5. Daluiski, A. et al. (2001) Nature Genetics 27:84.
Long Name
Bone Morphogenetic Protein 3
Entrez Gene IDs
651 (Human); 110075 (Mouse); 25667 (Rat)
Alternate Names
BMP3; BMP-3; BMP3A; BMP-3A; bone morphogenetic protein 3 (osteogenic); bone morphogenetic protein 3; Bone morphogenetic protein 3A; bone morphogenetic protein-3; Osteogenin

Citations for Recombinant Human BMP-3 Protein, CF

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. 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., 2011-07-07;286(34):30034-46.
    Species: Human, Mouse
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance
  2. BMP-3 promotes mesenchymal stem cell proliferation through the TGF-beta/activin signaling pathway.
    Authors: Stewart A, Guan H, Yang K
    J. Cell. Physiol., 2010-06-01;223(3):658-66.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  3. New role of bone morphogenetic protein 7 in brown adipogenesis and energy expenditure.
    Authors: Tseng YH, Kokkotou E, Schulz TJ, Huang TL, Winnay JN, Taniguchi CM, Tran TT, Suzuki R, Espinoza DO, Yamamoto Y, Ahrens MJ, Dudley AT, Norris AW, Kulkarni RN, Kahn CR
    Nature, 2008-08-21;454(7207):1000-4.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Xenopus neurula left-right asymmetry is respeficied by microinjecting TGF-beta5 protein.
    Authors: Mogi K, Goto M, Ohno E, Azumi Y, Takeuchi S, Toyoizumi R
    Int. J. Dev. Biol., 2003-02-01;47(1):15-29.
    Species: Xenopus
    Sample Types: In Vivo
    Applications: In Vivo

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