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Recombinant Human BMP-4 GMP Protein (rp164886-GMP) - Protein Bioactivity
Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells. The ED50 for this effect is approximately 95 ng/mL.
ActiBioPure™,His标签,无动物源,无载体,生物活性,高性能 级 提供 ≥95%(SDS-PAGE) 纯度,适用于对基线干扰要求严格的色谱和分析工作流程。
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在色谱分析、有机合成和交叉偶联反应领域已被 0 篇同行评审文献引用。
物理外观: Liquid
骨形态发生蛋白(Bone morphogenetic protein,BMPs)是转化生长因子β(TGF-β)超家族中的一员,继1965年Urist等学者首次从脱钙骨中提取出一类有助于成骨的蛋白成分之后,又陆续发现了多种骨形态发生蛋白,并发现了其促进成骨的作用。其中,人骨形态发生蛋白-4(BMP-4)作为BMPs家族成员之一,在空间结构上与BMPs大体结构有一致性,只有在成熟区序列方面有其特异性。BMP-4在促进骨组织再生修复方面发挥着重要作用。此外,BMP4也与诱导胚胎分化、指导神经干细胞分化、调节肿瘤生长侵袭以及一些心脑血管疾病密切相关。BMP4前蛋白原由400-500个氨基酸组成,包括3个部分:N-末端信号肽、前蛋白折叠区和C-末端成熟肽。羧基末端成熟的BMP4蛋白可在Furin,PC6和PC7的作用下,从前蛋白原上切割下来,成为由116个氨基酸组成的具有高度保守性的BMP4分子。它的C-末端含有7个半光氨酸残基,其中6个形成3个分子内二硫键,称为半胱氨酸结,第7个半胱氨酸可发生糖基化,借此形成共价二硫键用于与另一个单体二聚化,从而形成生物活性信号分子。
Bone morphogenetic proteins (BMPs) are members of the transforming growth factor beta (TGF - β) superfamily. After Urist and other scholars first extracted a class of osteogenic protein components from decalcified bone in 1965, various bone morphogenetic proteins have been discovered, and their role in promoting osteogenesis has been discovered. Among them, human bone morphogenetic protein-4 (BMP-4), as a member of the BMPs family, has spatial consistency with the general structure of BMPs, except for its specificity in the mature region sequence. BMP-4 plays an important role in promoting bone tissue regeneration and repair. In addition, BMP4 is closely related to inducing embryonic differentiation, guiding neural stem cell differentiation, regulating tumor growth and invasion, and some cardiovascular and cerebrovascular diseases. The BMP4 precursor protein is composed of 400-500 amino acids, including three parts: N-terminal signal peptide, precursor protein folding region, and C-terminal mature peptide. The carboxyl terminal mature BMP4 protein can be cleaved from the precursor protein by Furin, PC6, and PC7, becoming a highly conserved BMP4 molecule consisting of 116 amino acids. Its C-terminus contains 7 cysteine residues, of which 6 form 3 intramolecular disulfide bonds called cysteine bonds. The 7th cysteine can undergo glycosylation, forming a covalent disulfide bond for dimerization with another monomer, thereby forming a biologically active signaling molecule.
Recombinant Human BMP-4 GMP Protein (rp164886-GMP) - Protein Bioactivity
Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells. The ED50 for this effect is approximately 95 ng/mL.
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