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Description: BMP-2 is one of fifteen bone morphogenetic proteins (BMP) belonging to the TGF-beta superfamily. The BMPs were first identified as the active factors in demineralized bone matrix, with transcripts later being discovered in many other types of tissue. They are synthesized as large precursor molecules that must be cleaved into their active form and dimerize in order to exhibit functional activity. These dimers may include two identical or distinct BMP chains. BMP responsiveness appears to be limited to multipotent and immature cells. The BMPs are essential for osteogenesis and organogenesis during embryonic development, and also play a role in fracture and wound healing in adults.
Applications Reported: Human BMP-2 Recombinant Protein is biologically active.
Applications Tested: The ED50 of this protein, as determined by alkaline phosphatase induction in C3H/10T1/2 cells, is 0.25-1 µg/mL. This corresponds to a specific activity of 4x10e3 - 1x10e3 Units/mg.
Source: E. coli expressed amino acids Gln283-Arg396 accession number NP_001191.
Bioactivity: The ED50 of this protein, as determined by alkaline phosphatase induction in C3H/10T1/2 cells, is 0.25-1 ug/mL. This corresponds to a specific activity of 4x10e3 - 1x10e3 Units/mg.
Endotoxin: Less than 0.01 ng/ug cytokine as determined by the LAL assay. Purity: >97% as determined by SDS-PAGE.
Molecular Weight: 13 kDa.
Storage and handling: For best recovery, quick-spin vial prior to opening. Use in a sterile environment.
Purity: Greater than 90%, as determined by SDS-PAGE.
Aggregation: Less than 10%, as determined by HPLC.
Filtration: 0.2 µm post-manufacturing filtered.
Bone Morphogenic Proteins (BMP) are members of the TGF-beta superfamily that affect bone and cartilage formation (Hogan 1996, Reddi 1998 and Francis-West et al. 1999). 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 (Mundy et al. 1999). BMPs stimulate the production of specific bone matrix proteins and alter stromal cell and osteoclast proliferation (Macias et al. 1999, Lecanda et al. 1997). BMPs may also be an important factor for development of the viscera, with roles in cell proliferation, apoptosis, differentiation, and morphogenesis (Hogan 1996, Dale and Wardle 1999). 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 (Massague 1994, Derynck 1997, Attisano 1993).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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