Bone Morphogenetic Protein 2
Bone Morphogenetic Protein 2 (BMP-2) is a ligand protein with pleiotropic, belongs to TNFβ family. BMP-2 formats BMP/TGFβ signaling to involve in vascular and valvular homeostasis, which is a critical process of embryonic development[1]. BMP-2/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]. BMP-2 is widely found in different animals, while the sequence in human is similar to Rat (91.86%), and mouse (92.13%). BMPs exhibits critical contributions to the pathophysiology of atherosclerosis, pulmonary vascular disease, and vascular and valvular calcification[1]. BMP-2 binds different receptor, such as type I receptors (ALK-2/-3/-6) and type II receptors (BMPR2, ACVR2A), to regulate various calcification type[1]. BMP-2 promotes monocyte infiltration and inflammation of atherosclerotic legions[3]. It is linked to increased plaque formation via pro-inflammatory and pro-atherogenic effects, promoting oxidative stress, endothelial dysfunction and osteogenic differentiation[4]. BMP-2 is overexpressed in ossified regions of human calcified valves by myofibroblasts and pre-osteoblasts in areas densely infiltrated with B- and T-lymphocytes[5]. And it serves as the linkers between atherosclerotic vascular calcification with mechanisms of normal bone formation[6]. BMP-2 induces angiogenesis, endothelial cells (ECs) proliferation, and migration[7]. And BMP-2 also enhances the expression of the osteoblast and chondrocyte master transcriptional regulator RUNX2 to promote the mineralization of cultured human coronary vascular SMCs in a manner that was dependent on oxidative stress and endoplasmic reticulum (ER) stress[8].
- [1]. Yang P, et al. The role of bone morphogenetic protein signaling in vascular calcification. Bone. 2020 Dec;141:115542. [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]. Simões Sato AY, et al. BMP-2 and -4 produced by vascular smooth muscle cells from atherosclerotic lesions induce monocyte chemotaxis through direct BMPRII activation. Atherosclerosis. 2014 Jul;235(1):45-55. [Content Brief]
- [4]. Boström K, et al. Bone morphogenetic protein expression in human atherosclerotic lesions. J Clin Invest. 1993 Apr;91(4):1800-9. [Content Brief]
- [5]. Mohler ER 3rd, et al. Bone formation and inflammation in cardiac valves. Circulation. 2001 Mar 20;103(11):1522-8. [Content Brief]
- [6]. Demer LL, et al. Mechanism of calcification in atherosclerosis. Trends Cardiovasc Med. 1994 Jan-Feb;4(1):45-9. [Content Brief]
- [7]. David L, et al. Emerging role of bone morphogenetic proteins in angiogenesis. Cytokine Growth Factor Rev. 2009 Jun;20(3):203-12. [Content Brief]
- [8]. Liberman M, et al. Bone morphogenetic protein-2 activates NADPH oxidase to increase endoplasmic reticulum stress and human coronary artery smooth muscle cell calcification. Biochem Biophys Res Commun. 2011 Sep 30;413(3):436-41. [Content Brief]
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Bone Morphogenetic Protein 2 Recombinant Proteins (6)
- Species:
- Source:
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- 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.
