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|+1 404 474 4654|
|+1 888 205 9894 (TF)|
Bone Morphogenetic Protein 4 (BMP4) antibody
|Synonyms||ZYME, BMP2B, OFC11, BMP2B1, MCOPS6, Bmp-4, Bmp2b, Bmp2b1, Bmp2b-1, BOMPR4A, bmp-4, zbmp-4, MGC100779, zgc:100779, BMP4, BMP-4, xbmp4, XBMP-4, Bmp4, MGC127497, zyme, bmp2b, bmp2b1, bmp4|
Alternatives Neutralization (Neut), Western Blotting (WB), ELISA
|9 references available|
|Quantity||0.1 mg (0.5 mg/ml)|
|Price||Product not available in this region.|
|Immunogen||Recombinant full length protein expressed in NSO cells (Human).|
|Description||Bone Morphogenic Proteins (BMP) are members of the TGF-beta superfamily that affect bone and cartilage formation (1,2,3). Mature BMPs are 30-38 kDa proteins that assume a TGF-beta -like cysteine knot configuration. Lovostatin increases bone formation by turning on the bmp-2 gene (4). BMPs stimulate the production of specific bone matrix proteins and alter stromal cell and osteoclast proliferation (5,6). BMPs may also be an important factor for development of the viscera, with roles in cell proliferation, apoptosis, differentiation, and morphogenesis (1,7). BMPs appear to be responsible for normal dorsal/ventral patterning. Like TGF-beta, BMPs bind to a type II receptor, which then recruits the transducing type I receptor unit, activating the Smad protein signaling pathway (8,9,10).|
|Specificity||Monoclonal Anti-BMP-4 neutralizes human BMP-4, and recognizes recombinant human BMP-4 by ELISA and immunoblotting. The antibody shows approximately 5% cross-reactivity with recombinant human BMP-2, recombinant mouse BMP RIA and BMP-RIB.|
|Application Notes||I-ELISA: Use at a concentration of 0.5-1.0 ug/ml detects a limit of around 6 ng/well of human BMP-4. Neut: Use at a concentration of 1-3 ug/ml to neutralise 50% of the bioactivity due to 0.5 ug/ml recombinant human BMP-4I-WB: Use at a concentration of 1-2 ug/ml (using human BMP-4 at 50 ng/lane under non-reducing and reducing conditions). Not tested in other applications. Optimal dilutions/concentrations should be determined by the end user.|
|Purification||Protein G affinity purified|
|Storage||Store at 4 C. Aliquot and store at -20 C long-term. Avoid repeated freezing and thawing|
|Research Area||Organogenesis, Growth Factors, Angiogenesis, Signaling|
|Restrictions||For Research Use only|
Attisano, Cárcamo, Ventura et al.: "Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors." in: Cell, Vol. 75, Issue 4, pp. 671-80, 1993 (PubMed).
Hogan: "Bone morphogenetic proteins: multifunctional regulators of vertebrate development." in: Genes & development, Vol. 10, Issue 13, pp. 1580-94, 1996 (PubMed).
Lecanda, Avioli, Cheng: "Regulation of bone matrix protein expression and induction of differentiation of human osteoblasts and human bone marrow stromal cells by bone morphogenetic protein-2." in: Journal of cellular biochemistry, Vol. 67, Issue 3, pp. 386-96, 1997 (PubMed).
Derynck, Feng: "TGF-beta receptor signaling." in: Biochimica et biophysica acta, Vol. 1333, Issue 2, pp. F105-50, 1997 (PubMed).
Reddi: "Role of morphogenetic proteins in skeletal tissue engineering and regeneration." in: Nature biotechnology, Vol. 16, Issue 3, pp. 247-52, 1998 (PubMed).
Macias, Ganan, Rodriguez-Leon et al.: "Regulation by members of the transforming growth factor beta superfamily of the digital and interdigital fates of the autopodial limb mesoderm." in: Cell and tissue research, Vol. 296, Issue 1, pp. 95-102, 1999 (PubMed).
Francis-West, Parish, Lee et al.: "BMP/GDF-signalling interactions during synovial joint development." in: Cell and tissue research, Vol. 296, Issue 1, pp. 111-9, 1999 (PubMed).
Dale, Wardle: "A gradient of BMP activity specifies dorsal-ventral fates in early Xenopus embryos." in: Seminars in cell & developmental biology, Vol. 10, Issue 3, pp. 319-26, 1999 (PubMed).
Mundy, Garrett, Harris et al.: "Stimulation of bone formation in vitro and in rodents by statins." in: Science (New York, N.Y.), Vol. 286, Issue 5446, pp. 1946-9, 1999 (PubMed).