BMP-2 Protein, Human/Mouse/Rat

Bone morphogenetic protein 2 (BMP-2) is a pleiotropic ligand protein belonging to TNFβ family, and is involved in key embryonic development of vascular and valvular homeostasis. BMP-2 binds to type I receptors (ALK-2/-3/-6) and type II receptors (BMPR2, ACVR2A) to regulate various types of calcification, including atherosclerosis, chronic kidney disease, diabetes, and valve calcification^[1]. BMP-2 is overexpressed by myofibroblast and preosteoblast in the calcified area of human calcified valve, which are densely infiltrated by B lymphocytes and T lymphocytes^[2]. BMP-2 is the junction between atherosclerotic vascular calcification and normal bone formation mechanism^[3]. BMP-2 Protein, Human/Mouse/Rat is 114 a.a. (Q283-R396), expressed in E. coli.

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^[4].
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 including Atherosclerosis, Chronic Kidney Disease, Diabetes, Valvular Calcification^[1].
BMP-2 promotes monocyte infiltration and inflammation of atherosclerotic legions^[5].
It is linked to increased plaque formation via pro-inflammatory and pro-atherogenic effects, promoting oxidative stress, endothelial dysfunction and osteogenic differentiation^[6].
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^[2].
And it serves as the linkers between atherosclerotic vascular calcification with mechanisms of normal bone formation^[3].
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].

BMP-2 (10 nM; 15 min) shows little effect on the phosphorylation of MADR1, indicating MADR1 is a downstream component in the BMP2 signal transduction pathway^[9].
BMP-2 (50 ng/mL; 14 d) induces osteogenic differentiation of mesenchymal stem cells (MSCs) as well as strong synergistic effect with 1 ng/mL VEGF and 10 ng/mL bFGF, in bone marrow of femurs and tibias of 6 week-old rats^[10].

1. Measured by its ability to induce alkaline phosphatase production by ATDC-5 Cells. The ED₅₀ for this effect is typically <0.2 µg/mL.
2. Measured by its ability to induce alkaline phosphatase production by C2C12 cells. The ED₅₀ for this effect is typically <1 µg/mL.

Human; Rat; Mouse

E. coli

Tag Free

P12643 (Q283-R396)

650  [NCBI]

QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR

Approximately 26 kDa

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

Lyophilized powder

Lyophilized after extensive dialysis against 50 mM acetic acid.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in 20 mM HAc or diluted with 5 mM HCl.

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]. 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]

  [9]. Hoodless PA, et al. MADR1, a MAD-related protein that functions in BMP2 signaling pathways. Cell. 1996 May 17;85(4):489-500.  [Content Brief]

  [10]. Bai Y, et al. BMP-2, VEGF and bFGF synergistically promote the osteogenic differentiation of rat bone marrow-derived mesenchymal stem cells. Biotechnol Lett. 2013 Mar;35(3):301-8.  [Content Brief]