BMP-2 Protein, Human/Mouse/Rat
Based on 21 publication(s) in Google Scholar
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. 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. BMP-2 is the junction between atherosclerotic vascular calcification and normal bone formation mechanism. BMP-2 Protein, Human/Mouse/Rat is 114 a.a. (Q283-R396), expressed in E. coli.
- Species: Rat; Mouse; Human
- Source: E. coli
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Storage:Stored at -20°C for 2 years from date of receipt. 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.
Biological Activity
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.
Publications (21)
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Journal Impact Factor
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Most Recent
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Cell
Sex-dependent effects in the aged melanoma tumor microenvironment influence invasion and resistance to targeted therapy. [Abstract]2024 Oct 17;187(21):6016-6034.e25. PMID: 39243764
BMP-2 Protein, Human/Mouse/Rat purchased from MedChemExpress. Usage Cited in: Cell. 2024 Oct 17;187(21):6016-6034.e25. [Abstract]
Immunoblot for recombinant BMP2 (rBMP2) treatment in melanoma lines at indicated concentrations (for 30 minutes) showed changes in protein expression.
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Sci Bull
Enhanced osteochondral repair with hyaline cartilage formation using an extracellular matrix-inspired natural scaffold. [Abstract]2023 Sep 15;68(17):1904-1917. PMID: 37558534 -
Adv Sci (Weinh)
2024 Mar;11(10):e2308072. PMID: 38239021
BMP-2 Protein, Human/Mouse/Rat purchased from MedChemExpress. Usage Cited in: Adv Sci (Weinh). 2024 Mar;11(10):e2308072. [Abstract]
The immunofluorescence of pSmad1/5/8 was assessed 24 h after photostimulation, BMP2 (100 ng/mL; 24 h) treated (n = 16 fields in 3 independent trials for each group), with or without BMPR-I inhibitor LDN193189 (1 μM) and BMP ligand antagonist noggin (100 ng/mL), compared with the control group.
BMP-2 Protein, Human/Mouse/Rat purchased from MedChemExpress. Usage Cited in: Adv Sci (Weinh). 2024 Mar;11(10):e2308072. [Abstract]
The phosphorylated Smad 2 (pSmad2) expression level in ADSCs 3 h and 24 h after photostimulation, BMP2 (100 ng/mL) and DEX (10 nM) treated (n = 16 fields in 3 independent trials for each group) was measured.
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Mater Today Bio
Magnetic microspheres mimicking certain functions of macrophages: Towards precise antibacterial potency for bone defect healing. [Abstract]2023 May 1:20:100651. PMID: 37206878 -
J Orthop Translat
Oncostatin-M functionalized cryogel microspheres for promoting diabetic bone defects regeneration. [Abstract]2025 Jun 20:53:138-148. PMID: 40606844 -
J Mater Chem B
Development and in vitro/ in vivo evaluation of a triply periodic minimal surface-based 3D-printed anti-infective bone scaffold with spatiotemporally controlled osteogenesis. [Abstract]2025 Dec 3;13(47):15397-15412. PMID: 41235482 -
ACS Biomater Sci Eng
Low-Temperature Three-Dimensional Bioprinted Dual-Factor rhBMP-2/VEGF-165 Biomimetic Scaffolds for Synergistic Bone-Vascularization Repair in Large Segmental Bone Defect. [Abstract]2025 Dec 8;11(12):7357-7367. PMID: 41171637 -
Colloids Surf B Biointerfaces
A three-stage differentiation method for generating induced mesenchymal stem cells from human pluripotent stem cells via gelatin-based screening. [Abstract]2025 Nov 28:259:115324. PMID: 41349379 -
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Int J Mol Sci
Transcriptomics and Metabolomics Insights into the Dysregulation of Chondrocyte Differentiation Induced by T-2 Toxin. [Abstract]2025 Dec 9;26(24):11858. PMID: 41465285
BMP-2 Protein, Human/Mouse/Rat purchased from MedChemExpress. Usage Cited in: Int J Mol Sci. 2025 Dec 9;26(24):11858. [Abstract]
Expression patterns of key chondrocyte differentiation-related genes in ATDC5 cells following T-2 toxin and BMP2 (100 ng/mL; 48 h) recombinant protein intervention were analyzed.
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Sci Rep
Co-delivery of NGF and BMP-2 via thermosensitive pluronic F127 hydrogel enhances chondrogenesis and cartilage repair. [Abstract]2025 Sep 29;15(1):33354. PMID: 41023083 -
Biosci Rep
MiR-128 inhibits the osteogenic differentiation in osteoporosis by down-regulating SIRT6 expression. [Abstract]2019 Sep 24;39(9):BSR20191405. PMID: 31477582
BMP-2 Protein, Human/Mouse/Rat purchased from MedChemExpress. Usage Cited in: Biosci Rep. 2019 Sep 24;39(9):BSR20191405. [Abstract]
Determination of the expression of miR-128 in C2C12 cells treated with BMP-2 (2 nM) at days 0, 5, 10, and 21 by qRT-PCR was performed.
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Carcinogenesis
Long noncoding RNA MALAT1 sponging miR-26a-5p to modulate Smad1 contributes to colorectal cancer progression by regulating autophagy. [Abstract]2021 Nov 12;42(11):1370-1379. PMID: 34313719 -
Cell Biol Int
CoCl2 -simulated hypoxia potentiates the osteogenic differentiation of fibroblasts derived from tympanosclerosis by upregulating the expression of BMP-2. [Abstract]2022 Sep;46(9):1423-1432. PMID: 35811437 -
In Vitro Cell Dev Biol Anim
SOX2 suppresses osteoblast differentiation of MC3T3-E1 cells through activating the transcription of LGR4. [Abstract]2023 Jan;59(1):1-9. PMID: 36547788 -
Comput Math Methods Med
Effects of Coculture Fibroblasts and Vascular Endothelial Cells on Proliferation and Osteogenesis of Adipose Stem Cells. [Abstract]2022 Jan 13:2022:6288695. PMID: 35069787 -
Prog Biomater
Delivery of bone morphogenetic protein-2 by crosslinking heparin to nile tilapia skin collagen for promotion of rat calvaria bone defect repair. [Abstract]2023 Mar;12(1):61-73. PMID: 36495399 -
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Technical Parameters
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Species Rat; Mouse; Human
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Source E. coli
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Tag Tag Free
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Accession
P12643 (Q283-R396)
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Molecular Construction
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N-term
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BMP-2 (Q283-R396)
Accession # P12643 -
C-term
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Protein Length
Full Length of Mature Protein
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Synonyms
BMP2; SSFSC1; Prev. BMP2A; SSFSC; Bone Morphogenetic Protein 2A; BMP-2; BMP2 Protein; BDA2; Bone Morphogenetic Protein 2; BMP-2A
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AA Sequence
QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
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Molecular Weight
Approximately 13 kDa under reduced (R) conditions, 26 kDa under non reducing (N) conditions, based on SDS-PAGE.
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Structure/Form
Homodimer
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder
1.Lyophilized from a 0.22 μm filtered solution of 50 mM acetic acid.
2.Lyophilized from a 0.22 μm filtered solution of 50 mM acetic acid, pH 4.0, 5% mannitol.
Please refer to the lot-specific COA for specific buffer information.
<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. 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 from date of receipt. 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.
Documentation
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Data Sheet (265 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
References
[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]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)