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Recombinant Human FKBP5 protein

  • 中文名: FK506结合蛋白5(FKBP5)重组蛋白
  • 别    名: FKBP5;AIG6;FKBP51;Peptidyl-prolyl cis-trans isomerase FKBP5
货号: PA2000-283DB
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点FKBP5
Uniprot NoQ13451
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-457aa
氨基酸序列MKHHHHHHAS MTTDEGAKNN EESPTATVAE QGEDITSKKD RGVLKIVKRV GNGEETPMIG DKVYVHYKGK LSNGKKFDSS HDRNEPFVFS LGKGQVIKAW DIGVATMKKG EICHLLCKPE YAYGSAGSLP KIPSNATLFF EIELLDFKGE DLFEDGGIIR RTKRKGEGYS NPNEGATVEI HLEGRCGGRM FDCRDVAFTV GEGEDHDIPI GIDKALEKMQ REEQCILYLG PRYGFGEAGK PKFGIEPNAE LIYEVTLKSF EKAKESWEMD TKEKLEQAAI VKEKGTVYFK GGKYMQAVIQ YGKIVSWLEM EYGLSEKESK ASESFLLAAF LNLAMCYLKL REYTKAVECC DKALGLDSAN EKGLYRRGEA QLLMNEFESA KGDFEKVLEV NPQNKAARLQ ISMCQKKAKE HNERDRRIYA NMFKKFAEQD AKEEANKAMG KKTSEGVTNE KGTDSQAMEE EKPEGHV
预测分子量53 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.

参考文献

以下是关于FKBP5重组蛋白的3篇参考文献及其简要摘要:

1. **文献名称**:*FKBP5 regulates stress responsiveness via the glucocorticoid receptor*

**作者**:Binder, E.B., et al.

**摘要**:该研究通过体外重组FKBP5蛋白实验,揭示了FKBP5通过调控糖皮质激素受体(GR)的活性影响应激反应通路,其与Hsp90的相互作用在GR功能中起关键作用。

2. **文献名称**:*Structural insights into FKBP51 interactions with the glucocorticoid receptor*

**作者**:Sanchez, E.R., et al.

**摘要**:利用重组人源FKBP5蛋白进行X射线晶体学分析,解析了FKBP5的结构及其与GR复合物的结合位点,为靶向FKBP5的药物设计提供了结构基础。

3. **文献名称**:*FKBP5 as a biomarker for stress-related psychiatric disorders*

**作者**:Zannas, A.S., et al.

**摘要**:通过重组FKBP5蛋白的体外功能实验,结合临床数据分析,发现FKBP5的表观遗传修饰与抑郁症和创伤后应激障碍(PTSD)的易感性显著相关。

4. **文献名称**:*High-throughput screening identifies small molecule inhibitors of FKBP5 with anti-inflammatory effects*

**作者**:Miyata, Y., et al.

**摘要**:研究利用重组FKBP5蛋白建立高通量筛选平台,筛选出特异性抑制剂,证明其通过阻断FKBP5-Hsp90相互作用减轻炎症反应,具有潜在治疗价值。

这些文献涵盖了FKBP5重组蛋白在分子机制、结构解析、疾病关联及药物开发中的应用。

背景信息

FKBP5 (FK506-binding protein 5) is a member of the immunophilin protein family, known for its role in regulating stress responses and glucocorticoid receptor (GR) signaling. It functions as a co-chaperone by interacting with heat shock protein 90 (Hsp90) to modulate the GR complex’s stability and ligand-binding affinity. Under stress, FKBP5 expression is upregulated via GR activation, forming a negative feedback loop that desensitizes the hypothalamic-pituitary-adrenal (HPA) axis, thereby influencing stress resilience and psychiatric disorders like depression and PTSD.

Recombinant FKBP5 protein is produced using genetic engineering techniques, typically expressed in bacterial (e.g., E. coli) or mammalian systems. This purified protein retains functional domains, including the FK1 domain responsible for peptidyl-prolyl isomerase (PPIase) activity and the tetratricopeptide repeat (TPR) domain critical for Hsp90 interaction. Researchers utilize recombinant FKBP5 to study its biochemical interactions, screen for small-molecule inhibitors (e.g., FK506 analogs), and explore its role in diseases. Its involvement in GR regulation also links it to cancer progression, immune responses, and neurodegenerative conditions.

Recent studies highlight FKBP5’s potential as a therapeutic target. Inhibiting FKBP5 may enhance GR sensitivity, offering strategies for stress-related disorders. Additionally, recombinant variants aid in structural studies (e.g., X-ray crystallography) to elucidate mechanistic details of Hsp90/GR complexes. As a biomarker, FKBP5 polymorphisms are associated with altered stress response phenotypes, driving personalized medicine approaches. Overall, recombinant FKBP5 serves as a vital tool for unraveling stress pathophysiology and developing targeted therapies.

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