Bone Morphogenetic Protein 3 (BMP-3/Osteogenin)
Bone morphogenetic protein 3 (BMP-3, osteogenin) is paradoxically the most abundant BMP in bone yet functions predominantly as a negative regulator of bone formation rather than an osteogenic inducer. BMP-3 is a 472-amino-acid secreted TGF-β family member produced by osteoblasts and deposited in bone matrix; unlike BMP-2 or BMP-4, it does not productively engage the canonical BMP type I receptors ALK2/3/6, but instead binds activin receptor type II (ACVR2A/2B) and the type I receptor ALK4, activating SMAD2/3 rather than SMAD1/5/8. Through this activin-like signaling, BMP-3 antagonizes BMP-2-driven osteogenesis and restrains bone formation: BMP-3-null mice display increased bone density, while enhanced BMP-3 activity contributes to age-related and disuse bone loss. BMP-3 also regulates intestinal epithelial differentiation and has been detected in fetal tooth development and fracture healing. Its unique receptor usage among BMPs positions osteogenin as a distinct homeostatic brake on skeletal remodeling and a conceptual target for osteoporosis therapy.
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Bone Morphogenetic Protein 3 (BMP-3/Osteogenin) Recombinant Proteins (3)
- Species:
- Source:
Recombinant Protein Expression Service
- Codon Optimization
- Gene Synthesis
- Construction of Expression Vector
- Strain Screening
- Protein Expression
- Purification & QC
- Protein Delivery
- Formula: Human
- Molecular Weight: Sf9 insect cells
The EpCAM/TROP1 protein serves as an important homogeneous interacting molecule that promotes direct contact between intestinal epithelial cells (IEC) and intraepithelial lymphocytes (IEL) in the mucosal epithelium. This feature helps establish an immune barrier against mucosal infections. EpCAM/TROP1 Protein, Human (His-SUMO) is the recombinant human-derived EpCAM/TROP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
