首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Ngfb |
| Uniprot No | P01138 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 122-241aa |
| 氨基酸序列 | SSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA SSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA |
| 预测分子量 | 27 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Ngfb(神经生长因子β)重组蛋白的3篇代表性文献示例(内容为虚构，仅供参考)：
1. **文献名称**：*Expression and Purification of Recombinant Ngfb in E. coli*
**作者**：Smith A, et al.
**摘要**：该研究通过大肠杆菌表达系统成功制备了高纯度的重组Ngfb蛋白，并验证其促进神经元细胞存活的能力，为规模化生产提供了可行方案。
2. **文献名称**：*Ngfb Recombinant Protein Enhances Neuronal Regeneration in Vitro*
**作者**：Chen L, et al.
**摘要**：在体外模型中，重组Ngfb显著促进背根神经节神经元的轴突生长，证实其与天然Ngfb具有相似的生物活性，可用于神经退行性疾病研究。
3. **文献名称**：*Therapeutic Potential of Recombinant Ngfb in Diabetic Neuropathy*
**作者**：Wang X, et al.
**摘要**：通过小鼠糖尿病神经病变模型，发现重组Ngfb能有效缓解疼痛并改善周围神经功能，提示其作为临床治疗药物的潜力。
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**注**：以上文献为示例，实际引用需检索PubMed等数据库获取真实文献(可尝试关键词：*recombinant NGF beta* + expression/therapy/function*)。
Ngfb, also known as nerve growth factor-beta (β-NGF), is a member of the neurotrophin family critical for neuronal development, survival, and plasticity. Initially discovered in the 1950s for its role in sensory and sympathetic neuron growth, Ngfb binds to two receptors: the high-affinity tropomyosin receptor kinase A (TrkA) and the low-affinity p75 neurotrophin receptor (p75NTR). This dual-receptor interaction enables Ngfb to regulate diverse cellular processes, including axonal guidance, synaptic modulation, and inflammatory responses. Structurally, it exists as a homodimer stabilized by cysteine residues, a feature conserved across neurotrophins.
Recombinant Ngfb (rNgfb) is produced using genetic engineering techniques, typically expressed in bacterial (e.g., E. coli) or mammalian cell systems. Its recombinant form retains biological activity while offering scalability and purity for research and therapeutic applications. Studies employ rNgfb to investigate neurodegenerative diseases (e.g., Alzheimer’s, Parkinson’s), chronic pain mechanisms, and tissue regeneration. Notably, Ngfb’s role extends beyond neuroscience; it influences immune cell function and angiogenesis, implicating it in cancer progression and wound healing.
Therapeutic interest in rNgfb has grown, particularly for conditions like diabetic neuropathy and ocular diseases. However, its dual role in pain sensitization and neuroprotection presents challenges. Overexpression or dysregulation of Ngfb is linked to chronic pain and cancer metastasis, necessitating precise delivery systems. Current research explores engineered variants or targeted delivery platforms (e.g., nanoparticles) to mitigate off-target effects.
Despite hurdles like poor blood-brain barrier penetration and short half-life, advancements in protein engineering and gene therapy (e.g., CRISPR-modified Ngfb expression) hold promise. rNgfb remains a pivotal tool for unraveling neurotrophic mechanisms and developing precision therapies for neurological and systemic disorders.
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