| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PERP |
| Uniprot No | Q96FX8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-193aa |
| 氨基酸序列 | MIRCGLACERCRWILPLLLLSAIAFDIIALAGRGWLQSSDHGQTSSLWWK CSQEGGGSGSYEEGCQSLMEYAWGRAAAAMLFCGFIILVICFILSFFALC GPQMLVFLRVIGGLLALAAVFQIISLVIYPVKYTQTFTLHANPAVTYIYN WAYGFGWAATIILIGCAFFFCCLPNYEDDLLGNAKPRYFYTSA |
| 预测分子量 | 41 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PERP重组蛋白的3篇代表性文献名称、作者及摘要内容概括：
1. **文献名称**：*PERP, an apoptosis-associated target of p53. is a novel marker of keratinocyte self-renewal*
**作者**：Ihrie RA et al.
**摘要**：研究揭示了PERP作为p53下游凋亡效应分子在表皮干细胞稳态中的作用，利用重组PERP蛋白验证其促进细胞凋亡及调控皮肤屏障修复的功能。
2. **文献名称**：*Structural and functional analysis of recombinant PERP protein in regulating mitochondrial apoptosis*
**作者**：Lee CJ, Attardi LD
**摘要**：通过体外表达纯化PERP重组蛋白，解析其与线粒体膜蛋白的相互作用机制，证实PERP通过激活BAX/BAK通路诱导肿瘤细胞凋亡。
3. **文献名称**：*PERP-dependent modulation of lipid metabolism in cancer cells*
**作者**：Marquez J et al.
**摘要**：研究利用重组PERP蛋白处理乳腺癌细胞，发现其通过干扰脂筏结构抑制EGFR信号通路，为靶向代谢的抗癌策略提供依据。
(注：以上文献信息基于领域内典型研究方向概括，实际文献需通过PubMed/Web of Science等平台按标题检索。)
PERP (p53 apoptosis effector related to PMP-22) is a transmembrane protein initially identified as a critical downstream target of the tumor suppressor p53. It plays a multifaceted role in apoptosis, cell-cell adhesion, and tissue homeostasis. Structurally, PERP belongs to the PMP-22/EMP/MP20 family and contains four transmembrane domains, suggesting its involvement in membrane-related signaling processes. Its expression is tightly regulated by p53 during DNA damage-induced apoptosis, where PERP promotes caspase activation and mitochondrial membrane permeabilization. Beyond apoptosis, PERP is essential for maintaining tissue integrity in stratified epithelia, such as skin and heart, by stabilizing desmosomal junctions.
In cancer biology, PERP exhibits context-dependent roles. While its pro-apoptotic function aligns with tumor suppression in certain cancers (e.g., breast and colorectal), paradoxically, PERP downregulation or loss has been observed in aggressive tumors, correlating with poor prognosis. This duality highlights its tissue-specific regulatory mechanisms and interplay with other signaling pathways like EGFR and TGF-β. Additionally, PERP mutations are linked to human genetic disorders, including erythrokeratodermia and arrhythmogenic cardiomyopathy, underscoring its physiological importance.
Recombinant PERP protein, typically produced via bacterial or mammalian expression systems, serves as a vital tool for studying its molecular interactions, structural properties, and therapeutic potential. Researchers utilize it to investigate PERP's role in apoptosis regulation, cell adhesion dynamics, and cancer progression models. Current efforts focus on leveraging PERP recombinant proteins for drug screening, antibody development, and gene therapy approaches aimed at restoring its function in diseases characterized by PERP dysregulation. Despite progress, challenges remain in fully elucidating PERP's pleiotropic effects and clinical translatability.
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