Recombinant Human PIN1 protein

中文名： 肽基脯氨酰顺反式异构酶NIMA相互作用蛋白1(PIN1)重组蛋白
别名： PIN1;Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

货号: PA1000-2396

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>95%SDS-PAGE.
种属	Human
靶点	PIN1
Uniprot No	Q13526
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-163aa
氨基酸序列	MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQG EPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGE EDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPV FTDSGIHIILRTE
预测分子量	19 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3篇与PIN1重组蛋白相关的代表性文献及其摘要概述：

1. **文献名称**：*Role of the prolyl isomerase PIN1 in cell cycle regulation and cancer*

**作者**：Lu, K.P. et al.

**摘要**：该研究揭示了PIN1通过异构化磷酸化底物调控细胞周期进程的分子机制，并证明其异常表达与多种癌症相关，重组PIN1蛋白被用于验证其与Cyclin D1等蛋白的相互作用。

2. **文献名称**：*Structural basis for PIN1 catalytic activity and target recognition*

**作者**：Yeh, E.S. et al.

**摘要**：通过X射线晶体学解析了重组人源PIN1蛋白的三维结构，阐明了其催化结构域(PPIase)与底物结合的分子基础，为设计靶向抑制剂提供了结构依据。

3. **文献名称**：*PIN1 inhibition suppresses breast cancer progression via targeting oncogenic signaling*

**作者**：Rustighi, A. et al.

**摘要**：利用重组PIN1蛋白进行功能实验，发现抑制PIN1可阻断Notch和Wnt信号通路，抑制乳腺癌细胞增殖和转移，提示其作为治疗靶点的潜力。

4. **文献名称**：*PIN1 modulates tau phosphorylation and amyloidogenesis in Alzheimer's disease models*

**作者**：Nakatsu, Y. et al.

**摘要**：研究通过重组PIN1蛋白体外实验，证明其可调节tau蛋白的磷酸化状态，减少淀粉样斑块形成，为阿尔茨海默病的机制研究提供了新视角。

(注：以上文献标题和结论为领域典型研究方向概括，具体发表信息建议通过PubMed或Web of Science以“PIN1 recombinant protein”为关键词检索获取最新数据。)

背景信息

PIN1 (Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1) is a unique enzyme that regulates protein conformation and function by catalyzing the cis-trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motifs. Discovered in 1997. it belongs to the parvulin family of prolyl isomerases and plays a pivotal role in modulating cell cycle progression, signaling transduction, gene expression, and stress responses. PIN1 contains two functional domains: a WW domain for substrate recognition and a PPIase domain for catalytic activity. Its ability to alter protein structures post-phosphorylation allows it to act as a molecular switch, influencing diverse cellular processes including mitosis, apoptosis, and DNA damage repair.

PIN1 is implicated in multiple diseases, particularly cancer and neurodegenerative disorders. Overexpression of PIN1 is observed in numerous cancers, where it stabilizes oncoproteins (e.g., c-Myc, β-catenin) or inactivates tumor suppressors (e.g., p53), promoting tumorigenesis and metastasis. Conversely, reduced PIN1 activity is linked to Alzheimer’s disease, as it fails to prevent tau protein hyperphosphorylation and neurofibrillary tangle formation. These dual roles make PIN1 a compelling therapeutic target.

Recombinant PIN1 proteins are typically produced in Escherichia coli or mammalian expression systems for biochemical and structural studies. They enable researchers to investigate PIN1’s enzymatic mechanisms, substrate interactions, and inhibitor screening. Engineered variants (e.g., catalytic mutants like C113A) help dissect functional domains. In drug development, recombinant PIN1 facilitates the discovery of small-molecule inhibitors or stabilizers to modulate its activity in disease contexts. Recent studies also explore its role in immune regulation and viral infections, expanding its biomedical relevance.