Recombinant Human PPIL3 protein

中文名： 亲环蛋白J(PPIL3)重组蛋白
别名： PPIL3;Peptidyl-prolyl cis-trans isomerase-like 3

货号: PA1000-2479

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	PPIL3
Uniprot No	Q9H2H8
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-161aa
氨基酸序列	MGSSHHHHHHSSGLVPRGSHMSVTLHTDVGDIKIEVFCERTPKTCENFLA LCASNYYNGCIFHRNIKGFMVQTGDPTGTGRGGNSIWGKKFEDEYSEYLK HNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDE LEKLPVNEKTYRPLNDVHIKDITIHANPFAQ
预测分子量	20 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PPIL3重组蛋白的3篇参考文献的简要概括(注：文献信息为模拟示例，实际需根据真实文献调整)：

1. **文献名称**：Structural and functional analysis of PPIL3 in protein folding

**作者**：Chen L, et al.

**摘要**：本研究解析了重组人PPIL3蛋白的晶体结构，发现其通过肽酰脯氨酰异构酶活性参与内质网中胶原蛋白的折叠过程，并验证了其与HSP47的相互作用机制。

2. **文献名称**：PPIL3 regulates pre-mRNA splicing through U5 snRNP complex

**作者**：Wang Y, et al.

**摘要**：通过重组PPIL3蛋白的体外实验，揭示了其作为剪接体U5小核糖核蛋白复合物的调控因子，影响肿瘤细胞中VEGF等基因的可变剪接过程。

3. **文献名称**：PPIL3 deficiency disrupts T cell receptor signaling

**作者**：Kimura T, et al.

**摘要**：利用重组PPIL3蛋白进行的免疫共沉淀实验显示，该蛋白通过与CD3ε链相互作用调控T细胞受体信号转导，其缺失导致小鼠模型中出现自身免疫异常表型。

(注：实际文献需通过PubMed/Google Scholar等平台以"PPIL3 recombinant protein"为关键词检索获取，以上内容为领域常见研究方向模拟)

背景信息

PPIL3 (Peptidylprolyl Isomerase Like 3) is a member of the cyclophilin family, a group of proteins characterized by their ability to catalyze the cis-trans isomerization of proline peptide bonds, a critical step in protein folding and conformational regulation. This post-translational modification activity, known as PPIase (peptidylprolyl isomerase) activity, is essential for modulating protein structure, stability, and interactions. PPIL3 shares structural homology with other cyclophilins, particularly in its conserved cyclophilin-like domain, but exhibits distinct tissue expression patterns and functional roles.

Initially identified through genomic sequencing, PPIL3 is encoded in humans by the *PPIL3* gene located on chromosome 2. While its biological functions remain less characterized compared to well-studied cyclophilins like cyclophilin A (CypA), emerging evidence suggests PPIL3 involvement in transcriptional regulation, RNA splicing, and cellular stress responses. It interacts with components of the spliceosome complex, hinting at a role in mRNA processing. Additionally, PPIL3 may participate in signaling pathways linked to apoptosis and immune regulation, though mechanistic details are still under investigation.

Recombinant PPIL3 protein is engineered for in vitro studies to elucidate its biochemical properties and interactions. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), it retains PPIase activity and serves as a tool for structural analysis (e.g., X-ray crystallography) or screening for inhibitors. Its recombinant form is particularly valuable in dissecting its potential involvement in diseases such as cancer, neurodegenerative disorders, or viral infections, where cyclophilin dysregulation is implicated. Recent studies also explore PPIL3's utility as a biomarker or therapeutic target, though further functional validation is required to fully understand its pathophysiological relevance.