BMP-7
Bone Morphogenetic Protein 7 (BMP-7) is a ligand protein with pleiotropic, belongs to TGFβ family. BMP-7 is involved in regulating the proliferation, invasion and migration of cancer cells, associated with a variety of human tumors[1]. BMP-7 also appears to exhibit anti-inflammatory effects on the vasculature, and may function to maintain vascular integrity[2]. BMP-7 attenuates vascular calcification, but also corrects hyperphosphatemia associated with uremia, and stimulates orthotopic skeletal phosphate deposition while simultaneously preventing vascular calcification by direct action on vascular smooth muscle cells[3]. BMP/TGFβ signaling to involve in vascular and valvular homeostasis, which is a critical process of embryonic development[4]. BMP-7 inhibits primary human aortic smooth muscle cells (SMCs) proliferation due to stimulation with serum, platelet-derived growth factor subunit BB (PDGF-BB) or TGFβ1, and maintains the expression of the vascular SMC phenotype[2]. BMP-7 binds ALK2 or ACVR2A/BMPR2 to signal, and can be terminated by inhibitory SMADs including SMAD6 and SMAD7, which are activated and induced by BMP signaling and switch off BMP signaling via multiple mechanisms[5]. However, BMP-7 knockdown results the expression of p-Smad1/5/9 significantly decreased, accompanied with BMP-7-Smad1/5/9 signaling pathway inactive and epithelial-mesenchymal transition (EMT) process reverse[1]. In lung cancer, BMP-7 inhibits bone metastasis, and induces apoptosis and cell cycle arrest. In malignant melanoma, BMP-7 can induce mesenchymal-epithelial transformation and inhibit the metastasis of cancer cells. BMP-7 inhibit epithelial-mesenchymal transition (EMT)-related genes and cell invasion, inhibit telomerase, shorten telomeres, and induce the aging and apoptosis of breast cancer cells. BMP-7 increases the cell proliferation and migration potential in a model of metastatic breast cancer in the bone and prostate cancer[1]. BMP-7 is widely found in different animals, while the sequence in human is highly similar to Rat (98.08%), and Mouse (97.67%).
- [1]. Sun R, et al. Expression of BMP-7 in cervical cancer and inhibition of epithelial‑mesenchymal transition by BMP-7 knockdown in HeLa cells. Int J Mol Med. 2020 May;45(5):1417-1424. [Content Brief]
- [2]. Dorai H, et al. Bone morphogenetic protein-7 (osteogenic protein-1) inhibits smooth muscle cell proliferation and stimulates the expression of markers that are characteristic of SMC phenotype in vitro. J Cell Physiol. 2000 Jul;184(1):37-45. [Content Brief]
- [3]. Mathew S, et al. Function and effect of bone morphogenetic protein-7 in kidney bone and the bone-vascular links in chronic kidney disease. Eur J Clin Invest. 2006 Aug;36 Suppl 2:43-50. [Content Brief]
- [4]. Yang P, et al. The role of bone morphogenetic protein signaling in vascular calcification. Bone. 2020 Dec;141:115542. [Content Brief]
- [5]. Miyazawa K, et al. Regulation of TGF-β Family Signaling by Inhibitory Smads. Cold Spring Harb Perspect Biol. 2017 Mar 1;9(3):a022095. [Content Brief]
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BMP-7 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
- Formel: 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.
