| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NMB |
| Uniprot No | P08949 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-121aa |
| 氨基酸序列 | MARRAGGARMFGSLLLFALLAAGVAPLSWDLPEPRSRASKIRVHSRGNLWATGHFMGKKSLEPSSPSPLGTAPHTSLRDQRLQLSHDLLGILLLKKALGVSLSRPAPQIQYRRLLVQILQK |
| 预测分子量 | kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于脑膜炎奈瑟菌B型(Neisseria meningitidis serogroup B, NMB)重组蛋白的3篇代表性文献摘要：
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1. **文献名称**：*Expression and purification of recombinant Neisseria meningitidis outer membrane protein NMB in Escherichia coli*
**作者**：Adu-Bobie J. et al.
**摘要**：本研究在大肠杆菌中成功表达了NMB外膜蛋白的重组形式，并通过亲和层析纯化获得高纯度蛋白。实验验证其抗原性，为后续疫苗开发奠定基础。
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2. **文献名称**：*Immunogenicity of a recombinant protein containing the Neisseria meningitidis serogroup B vaccine candidate GNA2091*
**作者**：Giuliani M.M. et al.
**摘要**：作者构建了包含NMB抗原GNA2091的重组融合蛋白，在小鼠模型中证实其可诱导强效杀菌抗体，支持其作为多价脑膜炎疫苗组分的潜力。
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3. **文献名称**：*Structural characterization of the NMB1870 antigen from Neisseria meningitidis*
**作者**：Scarselli M. et al.
**摘要**：通过X射线晶体学解析了NMB1870重组蛋白的三维结构，揭示其表面暴露的抗原表位，为基于结构的疫苗设计提供关键信息。
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**注**：若您所指"NMB"为其他蛋白(如GPNMB)，请补充说明以便调整检索方向。
Neuromedin B (NMB), a 10-amino-acid neuropeptide belonging to the bombesin-like peptide family, plays critical roles in regulating physiological processes such as smooth muscle contraction, hormone secretion, and energy homeostasis. Initially isolated from porcine spinal cord in 1983. NMB interacts specifically with the neuromedin B receptor (NMBR), a G protein-coupled receptor (GPCR) expressed in the central nervous system and peripheral tissues. Its functional homolog, gastrin-releasing peptide (GRP), shares structural similarities but differs in receptor specificity and tissue distribution.
The development of recombinant NMB protein emerged as a pivotal tool for studying NMBR signaling mechanisms and therapeutic potential. Using recombinant DNA technology, researchers have engineered stable NMB variants in bacterial or mammalian expression systems, often incorporating fusion tags (e.g., His-tag) for purification. These recombinant proteins enable precise investigation of NMB's role in pathophysiological contexts, including its dual functions in cancer progression—acting as both a growth inhibitor in some tumors and a promoter in others through autocrine/paracrine pathways.
Recent studies highlight NMB's involvement in metabolic regulation and inflammatory responses, sparking interest in targeting the NMB-NMBR axis for treating obesity-related disorders and chronic inflammation. However, challenges remain in understanding receptor subtype cross-activation and developing clinically viable modulators. Recombinant NMB continues to serve as a cornerstone for structural studies, drug screening platforms, and biomarker research, bridging molecular insights with translational applications in endocrinology and oncology.
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