BMP-2 蛋白, Zebrafish

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.

骨形态发生蛋白2（BMP-2）是一种多效性配体蛋白，属于TGFβ家族。BMP-2 格式化 BMP/TGFβ 信号传导以参与血管和瓣膜稳态，这是胚胎发育的关键过程^[1]。
BMP-2/TGFβ 信号传导可通过抑制性终止SMAD 包括 SMAD6 和 SMAD7，它们由 BMP 信号传导激活和诱导，并通过多种机制关闭 BMP 信号传导^[2]。
BMP-2 广泛存在于不同动物中，而其序列人体中的情况与大鼠 (91.86%) 和小鼠 (92.13%) 相似。
BMP 对动脉粥样硬化、肺血管疾病以及血管和瓣膜钙化的病理生理学具有重要贡献^[1]。
BMP-2结合不同的受体，如I型受体（ALK-2/-3/-6）和II型受体（BMPR2、ACVR2A），调节多种钙化类型，包括动脉粥样硬化、慢性肾脏病、糖尿病、瓣膜钙化^[1]。
BMP-2 促进单核细胞浸润和动脉粥样硬化军团的炎症^[3]。
它与通过促炎和促动脉粥样硬化作用增加斑块形成，促进氧化应激、内皮功能障碍和成骨分化^[4]。
BMP-2 在人钙化瓣膜的骨化区域过表达B、T 淋巴细胞密集浸润区域的肌成纤维细胞和前成骨细胞^[5]。
是动脉粥样硬化血管钙化与正常骨形成机制之间的纽带 ^[6]。
BMP-2 诱导血管生成、内皮细胞 (EC) 增殖和迁移^[7]。
BMP-2 还能增强血管生成、内皮细胞 (EC) 增殖和迁移。成骨细胞和软骨细胞主转录调节因子 RUNX2 的作用，以依赖于氧化应激和内质网 (ER) 应激的方式促进培养的人冠状血管 SMC 的矿化^[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.

Others

E. coli

Tag Free

B3DI86 (Q272-R386)

/

QARNNKQRKKHKANCRRHSLYVDFSDVGWNDWIVAPPGYHAFYCQGECPFPLADHLNSTNHAIVQTLVNSVNSNIPRACCVPTDLSPVSLLYLDEYERVILKNYQDMVVEGCGCR

Approximately 13 kDa

Greater than 95% as determined by reducing SDS-PAGE

无菌粉末.

Lyophilized from a 0.2 μm filtered solution of 30 mM HAC, pH 3.0 or 50 mM Tris-HCL, 300 mM NaCl, 200 mM Arginine, pH 8.0.

<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. 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]