BMP-2 Protein, Zebrafish
Based on 2 publication(s) in Google Scholar
Bone morphogenetic protein 2 (BMP-2) is a pleiotropic ligand protein belonging to TGFβ 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. Zebrafish BMP-2 Protein has a length of 386 a.a., BMP-2 Protein, Zebrafish is 105 a.a. (Q272-R386), expressed in E. coli cells with tag free.
- Species: Others
- Source: E. coli
-
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.
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
-
Biological Activity
-
Technical Parameters
-
Product Properties
- Documentation
- References
- Help & FAQs
Biological Activity
Bone morphogenetic protein 2 (BMP-2) is a pleiotropic ligand protein belonging to TGFβ 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[5]. BMP-2 is the junction between atherosclerotic vascular calcification and normal bone formation mechanism[6]. Zebrafish BMP-2 Protein has a length of 386 a.a., BMP-2 Protein, Zebrafish is 105 a.a. (Q272-R386), expressed in E. coli cells with tag free.
Bone Morphogenetic Protein 2 (BMP-2) is a ligand protein with pleiotropic, belongs to TGFβ 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 including Atherosclerosis, Chronic Kidney Disease, Diabetes, Valvular Calcification[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. Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells and the ED50 is typically 0.5-3 μg/mL.
2. Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells. The ED50 for this effect is 48-400 ng/mL.
Publications (2)
-
Journal Impact Factor
-
Most Recent
-
iScience
SENP1 facilitates OM-MSC differentiation through activating OPTN-mediated mitophagy to mitigate the neurologic impairment following ICH. [Abstract]2024 Apr 30;27(6):109865. PMID: 38770132 -
Technical Parameters
-
Species Others
-
Source E. coli
-
Tag Tag Free
-
Accession
B3DI86 (Q272-R386)
-
Gene ID/
-
Molecular Construction
-
N-term
-
BMP-2 (Q272-R386)
Accession # B3DI86 -
C-term
-
-
Protein Length
Partial
-
Synonyms
BDA2; BMP-2; BMP-2A; Bone morphogenetic protein 2a; SSFSC
-
AA Sequence
QARNNKQRKKHKANCRRHSLYVDFSDVGWNDWIVAPPGYHAFYCQGECPFPLADHLNSTNHAIVQTLVNSVNSNIPRACCVPTDLSPVSLLYLDEYERVILKNYQDMVVEGCGCR
-
Predicted Molecular Mass
13.2 kDa
-
Molecular Weight
Approximately 13 kDa, based on SDS-PAGE under reducing conditions.
-
Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
Lyophilized from a 0.22 μm filtered solution of 30 mM HAC, pH 3.0, 5% trehalose, 5% mannitol, 0.01% Tween 80.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. 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
-
Data Sheet (264 KB)
-
SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
-
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]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
Powered by Bioz
