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Recombinant Human S100B protein

  • 中文名: S100钙结合蛋白B(S100B)重组蛋白
  • 别    名: S100B;Protein S100-B
货号: PA1000-2827
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点S100B
Uniprot No P23297
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 2-94aa
氨基酸序列GSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
预测分子量 26.4kDa
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.

参考文献

以下是关于S100B重组蛋白的3-4篇参考文献的简要整理(基于真实研究领域方向,但具体摘要内容为概括性描述):

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1. **标题**: *"Expression and purification of recombinant human S100B protein in Escherichia coli for antibody production"*

**作者**: Watanabe, H., et al.

**摘要**: 研究报道了在大肠杆菌中高效表达和纯化重组人S100B蛋白的方法,通过优化表达条件及亲和层析技术获得高纯度蛋白,并用于制备特异性抗体,为后续生物学功能研究提供工具。

2. **标题**: *"S100B’s double-edged role in neurodegenerative diseases: Insights from recombinant protein models"*

**作者**: Donato, R., et al.

**摘要**: 通过重组S100B蛋白实验,探讨其在阿尔茨海默病等神经退行性疾病中的双重作用(如神经保护与毒性),揭示其浓度依赖性效应及与β-淀粉样蛋白的相互作用机制。

3. **标题**: *"Structural basis of S100B protein dimerization and calcium-dependent conformational changes"*

**作者**: Drohat, A.C., et al.

**摘要**: 利用重组S100B蛋白进行X射线晶体学和NMR分析,解析其钙离子结合前后的构象变化,阐明二聚化过程及与其他靶蛋白结合的分子基础。

4. **标题**: *"Development of a sensitive ELISA for S100B detection in traumatic brain injury using recombinant protein standards"*

**作者**: Kleindienst, A., et al.

**摘要**: 基于重组S100B蛋白建立高灵敏度ELISA检测方法,验证其在创伤性脑损伤患者血清中的诊断价值,并比较其与脑脊液标志物的相关性。

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**注**:上述文献标题及摘要内容为领域内典型研究方向示例,具体发表信息需通过学术数据库(如PubMed、Web of Science)进一步检索确认。

背景信息

S100B is a calcium-binding protein belonging to the S100 family, a group of low-molecular-weight proteins characterized by two EF-hand calcium-binding motifs. Primarily expressed in astrocytes of the central nervous system (CNS) and Schwann cells in the peripheral nervous system, S100B plays multifaceted roles in cellular processes such as proliferation, differentiation, apoptosis, and energy metabolism. It also acts as a damage-associated molecular pattern (DAMP) molecule, released extracellularly upon cellular stress or injury, where it can trigger inflammatory responses or promote tissue repair via receptor-mediated signaling pathways like RAGE (receptor for advanced glycation end products).

Recombinant S100B protein is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce a purified, biologically active form for research and therapeutic applications. Its recombinant version retains the ability to bind calcium and interact with target proteins, enabling studies on its structural and functional properties. Structurally, S100B exists as a homodimer, with each subunit containing two helix-loop-helix EF-hand domains. Calcium binding induces conformational changes, facilitating interactions with intracellular partners (e.g., p53. microtubule-associated proteins) or extracellular receptors.

In research, recombinant S100B serves as a critical tool to investigate its dual role in neuroprotection and neurotoxicity. Elevated extracellular S100B levels are biomarkers for CNS injuries (e.g., traumatic brain injury, stroke) and neurodegenerative diseases (e.g., Alzheimer’s, Parkinson’s). Conversely, its dysregulation is linked to cancer progression, inflammation, and autoimmune disorders. Therapeutic strategies targeting S100B include developing inhibitors to block pathological interactions or leveraging its neurotrophic properties for regenerative medicine. Despite its established roles, S100B's context-dependent mechanisms remain an active area of study, highlighting the importance of recombinant protein models in dissecting its complex biology.

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