BMP-7 Protein, Human

Bone morphogenetic protein 7 (BMP-7) is a polymorphic ligand protein belonging to the TGFβ family. BMP-7 is involved in regulating the proliferation, invasion and migration of cancer cells and is associated with a variety of human tumors^[1]. BMP-7 binds ALK2 or ACVR2A/BMPR2 excitation signal, which is terminated by SMADs regulation^[2]. BMP-7 is involved in the BMP-7-SMad1/5/9 signaling pathway, which is associated with the epithelial-mesenchymal transition (EMT) process^[1]. BMP-7 also eliminates vascular inflammation, maintains vascular integrity^[3], reduces vascular calcification, and stimulates in situ phosphate ossification deposition^[4]. The total length of human BMP-7 protein is 431 amino acids (M1-H431), with 4 glycosylation domains. BMP-7 Protein, Human has a total length of 139 amino acids (S293-H431), is expressed in E. coli cells.

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^[3].
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^[4].
BMP/TGFβ signaling to involve in vascular and valvular homeostasis, which is a critical process of embryonic development^[5].
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^[3].
And BMP/TGFβ signaling 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^[2].
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 has also been found to increase 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 mouse is highly similar to rat (100.00%), and human (97.67%).

BMP-7 (300 ng/mL) initiates a synchronous wave of differentiation occurred, characterized by flattened, enlarged cells with reduced proliferation^[6].
BMP-7 (50 ng/mL; 1, 3, 5, 7, and 17 d) induces SCG neurons dendritic growth^[7].

Human

E. coli

Tag Free

P18075 (S293-H431)

655  [NCBI]

STGSKQRSQNRSKTPKNQEALRMANVAENSSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAYYCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKPCCAPTQLNAISVLYFDDSSNVILKKYRNMVVRACGCH

Approximately 15.7 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized after extensive dialysis against solution in 30% acetonitrile, 0.1% TFA.

<1.0 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in 10mM HAc. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [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]. 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]

  [3]. 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]

  [4]. 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]

  [5]. Yang P, et al. The role of bone morphogenetic protein signaling in vascular calcification. Bone. 2020 Dec;141:115542.  [Content Brief]

  [6]. Xu RH, et al. BMP4 initiates human embryonic stem cell differentiation to trophoblast. Nat Biotechnol. 2002 Dec;20(12):1261-4.  [Content Brief]

  [7]. Beck HN, et al. Bone morphogenetic protein-5 (BMP-5) promotes dendritic growth in cultured sympathetic neurons. BMC Neurosci. 2001;2:12.  [Content Brief]