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Recombinant human BMP-2 is a non-glycosylated homodimer, containing two 115 amino acid chains, with a molecular weight of 26 kDa. Purity is typically greater than 97% and endotoxin level less than 1 EU/ug.
The expected biological activity (ED50) is determined by the alkaline phosphatase activity induced in ATDC-5 cells and is typically 56-85 ng/mL. The specific activity of this protein is 2x10^3 units/mg.
Reconstitute using sterile water at 0.1 mg/mL and centrifuge prior to opening vial. Gently pipet solution down the sides of the vial. DO NOT VORTEX sample. Store reconstituted material at -20ºC and add 0.1% BSA for additional stability.
Amino acid sequence: MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISM LYLDENEKVV LKNYQDMVVE GCGCR.
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).
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