Bone Morphogenetic Protein 2 (BMP2) (AA 283-396) (Active) Protein Protein
BMP2 Spezies: Human Quelle: Escherichia coli (E. coli) Recombinant > 95 % as analyzed by non-reducing SDS-PAGE.
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- Biologische Aktivität
- AA 283-396
- Escherichia coli (E. coli)
- ED50 < 1 μg/mL, measured by alkaline phosphatase induction assay using C2C12 cells.
AA 283-396, expressed with an N-terminal Met.
- > 95 % as analyzed by non-reducing SDS-PAGE.
- < 1 EU/μg, determined by LAL method.
- Nur für Forschungszwecke einsetzbar
- Reconstituted in 20 mM AcOH or 5 mM HCl. The solubility should be at 100 μg/mL.
- Lyophilized after extensive dialysis against 50 mM acetic acid.
- -80 °C
- Informationen zur Lagerung
- Lyophilized recombinant human Bone Morphogenetic Protein-2 (rhBMP-2) remains stable up to 6 months at -80 °C from date of receipt. Upon reconstitution, rhBMP-2 should be stable up to 2 weeks at 4 °C or up to 3 months at -20 °C.
- 6 months
Wang, Park, La Marca, Than, Lin: "BMP-2 inhibits tumor-initiating ability in human renal cancer stem cells and induces bone formation." in: Journal of cancer research and clinical oncology, Vol. 141, Issue 6, pp. 1013-24, 2015 (PubMed).
Chanchareonsook, Tideman, Feinberg, Jongpaiboonkit, Lee, Flanagan, Krishnaswamy, Jansen: "Segmental mandibular bone reconstruction with a carbonate-substituted hydroxyapatite-coated modular endoprosthetic poly(?-caprolactone) scaffold in Macaca fascicularis." in: Journal of biomedical materials research. Part B, Applied biomaterials, Vol. 102, Issue 5, pp. 962-76, 2014 (PubMed).
Clark, Milbrandt, Hilt, Puleo: "Mechanical properties and dual drug delivery application of poly(lactic-co-glycolic acid) scaffolds fabricated with a poly(?-amino ester) porogen." in: Acta biomaterialia, Vol. 10, Issue 5, pp. 2125-32, 2014 (PubMed).
Alegre-Aguarón, Sampat, Xiong, Colligan, Bulinski, Cook, Ateshian, Brown, Hung: "Growth factor priming differentially modulates components of the extracellular matrix proteome in chondrocytes and synovium-derived stem cells." in: PLoS ONE, Vol. 9, Issue 2, pp. e88053, 2014 (PubMed).
Cushnie, Ulery, Nelson, Deng, Sethuraman, Doty, Lo, Khan, Laurencin: "Simple signaling molecules for inductive bone regenerative engineering." in: PLoS ONE, Vol. 9, Issue 7, pp. e101627, 2014 (PubMed).
Asai, Otsuru, Candela, Cantley, Uchibe, Hofmann, Zhang, Wapner, Soslowsky, Horwitz, Enomoto-Iwamoto: "Tendon progenitor cells in injured tendons have strong chondrogenic potential: the CD105-negative subpopulation induces chondrogenic degeneration." in: Stem cells (Dayton, Ohio), Vol. 32, Issue 12, pp. 3266-77, 2014 (PubMed).
Saldanha, Bragdon, Moseychuk, Bonor, Dhurjati, Nohe: "Caveolae regulate Smad signaling as verified by novel imaging and system biology approaches." in: Journal of cellular physiology, Vol. 228, Issue 5, pp. 1060-9, 2013 (PubMed).
Wang, Park, Zhang, La Marca, Claeson, Than, Rahman, Lin: "BMP-2 inhibits tumor growth of human renal cell carcinoma and induces bone formation." in: International journal of cancer. Journal international du cancer, Vol. 131, Issue 8, pp. 1941-50, 2012 (PubMed).
Darcy, Meltzer, Miller, Lee, Chappell, Ver Donck, Montano: "A novel library screen identifies immunosuppressors that promote osteoblast differentiation." in: Bone, Vol. 50, Issue 6, pp. 1294-303, 2012 (PubMed).
Sandberg, Eliasson, Andersson, Agholme, Aspenberg: "Etanercept does not impair healing in rat models of tendon or metaphyseal bone injury." in: Acta orthopaedica, Vol. 83, Issue 3, pp. 305-10, 2012 (PubMed).
Song, Yang, Park, Song, Han, Youn, Cho: "The role of histone chaperones in osteoblastic differentiation of C2C12 myoblasts." in: Biochemical and biophysical research communications, Vol. 423, Issue 4, pp. 726-32, 2012 (PubMed).
Li, Khavandgar, Lin, Murshed: "Lithium chloride attenuates BMP-2 signaling and inhibits osteogenic differentiation through a novel WNT/GSK3- independent mechanism." in: Bone, Vol. 48, Issue 2, pp. 321-31, 2011 (PubMed).
Shimono, Tung, Macolino, Chi, Didizian, Mundy, Chandraratna, Mishina, Enomoto-Iwamoto, Pacifici, Iwamoto: "Potent inhibition of heterotopic ossification by nuclear retinoic acid receptor-? agonists." in: Nature medicine, Vol. 17, Issue 4, pp. 454-60, 2011 (PubMed).
Jeon, Powell, Solorio, Krebs, Alsberg: "Affinity-based growth factor delivery using biodegradable, photocrosslinked heparin-alginate hydrogels." in: Journal of controlled release : official journal of the Controlled Release Society, Vol. 154, Issue 3, pp. 258-66, 2011 (PubMed).
Bragdon, Thinakaran, Moseychuk, Gurski, Bonor, Price, Wang, Beamer, Nohe: "Casein kinase 2 regulates in vivo bone formation through its interaction with bone morphogenetic protein receptor type Ia." in: Bone, Vol. 49, Issue 5, pp. 944-54, 2011 (PubMed).
- Wang, Park, La Marca, Than, Lin: "BMP-2 inhibits tumor-initiating ability in human renal cancer stem cells and induces bone formation." in: Journal of cancer research and clinical oncology, Vol. 141, Issue 6, pp. 1013-24, 2015 (PubMed).
- BDA2, BMP2A, AI467020, Bmp2a, BMP-2, xBMP-2, xbmp2, BMP2, bmp2a, bmp2, wu:fc59d09, bone morphogenetic protein 2, bone morphogenetic protein 2 L homeolog, Bone morphogenetic protein 2, bone morphogenetic protein 2a, BMP2, Bmp2, bmp2.L, bmp2, bmp2a
- Human Bone Morphogenetic Protein-2 (BMP-2) is a bone-growth regulatory factor and belongs to the transforming growth factor-beta (TGF-beta) superfamily. Human Bone Morphogenetic Protein-2 (BMP-2) is synthesized as large precursor molecule (Met1-Arg396, with a signal peptide from Met1 to Gly23), propeptide (Leu24-Arg282) of which is cleaved by PCSK5 (Proprotein Convertase Subtilisin/Kexin type 5). The active form consists of a dimer of two identical proteins which are linked by a disulfide bond at Cys360. It plays an important role in the development of bone and cartilage, cardiac cell differentiation and epithelial to mesenchymal transition. It is also involved in the hedgehog pathway, TGF-beta signaling pathway, and in cytokine-cytokine receptor interaction. Recombinant human Bone Morphogenetic Protein-2 (rhBMP-2) produced in E. coli is a disulfide-linked homodimer containing two non-glycosylated polypeptide chains of 115 amino acids. A fully biologically active molecule, rhBMP-2 has a molecular mass of 26 kDa analyzed by non-reducing SDS-PAGE.
Synonyms: BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2
- 26 kDa, observed by non-reducing SDS-PAGE
- Regulation of Hormone Metabolic Process, Regulation of Hormone Biosynthetic Process, Regulation of Muscle Cell Differentiation, Growth Factor Binding, Positive Regulation of fat Cell Differentiation
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