纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PDRG1 |
Uniprot No | Q9NUG6 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-133aa |
氨基酸序列 | MLSPEAERVLRYLVEVEELAEEVLADKRQIVDLDTKRNQNREGLRALQKDLSLSEDVMVCFGNMFIKMPHPETKEMIEKDQDHLDKEIEKLRKQLKVKVNRLFEAQGKPELKGFNLNPLNQDELKALKVILKG |
预测分子量 | 31.5kDa |
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PDRG1重组蛋白的3篇参考文献及其摘要概括:
1. **文献名称**: *"Cloning and characterization of PDRG1. a novel p53-responsive gene involved in cell growth regulation"*
**作者**: Smith A, et al.
**摘要**: 本研究首次克隆并鉴定了PDRG1基因,发现其在p53信号通路中被显著诱导表达。通过重组蛋白技术在大肠杆菌中表达并纯化了PDRG1蛋白,证实其能够抑制肿瘤细胞增殖,提示其在DNA损伤应答中的潜在调控作用。
2. **文献名称**: *"PDRG1 interacts with p53 and modulates its transcriptional activity in response to genotoxic stress"*
**作者**: Chen L, et al.
**摘要**: 研究利用重组人PDRG1蛋白进行体外结合实验,发现PDRG1直接与p53蛋白相互作用,并通过调控p53靶基因(如p21和BAX)的转录活性影响细胞凋亡。该结果为PDRG1在癌症治疗中的功能提供了分子机制依据。
3. **文献名称**: *"Recombinant PDRG1 protein suppresses tumor growth via regulating mTOR signaling pathway"*
**作者**: Wang Y, et al.
**摘要**: 通过昆虫表达系统制备了高纯度重组PDRG1蛋白,并在小鼠模型中验证其通过抑制mTOR通路抑制肿瘤生长的作用。研究进一步揭示了PDRG1作为肿瘤抑制因子的潜在治疗价值。
注:上述文献信息为示例性内容,实际研究中建议通过PubMed或Web of Science检索最新论文。
**Background of PDRG1 Recombinant Protein**
PDRG1 (p53 and DNA damage-regulated gene 1) is a gene regulated by the tumor suppressor protein p53 and cellular stress signals, notably DNA damage. Located on human chromosome 20q11.21. it encodes a 23 kDa protein implicated in diverse cellular processes, including cell cycle regulation, apoptosis, and tumor suppression. PDRG1 expression is induced under genotoxic stress, hypoxia, or oxidative stress, suggesting its role in stress response pathways. Studies link PDRG1 to p53-mediated pathways, where it may act as a downstream effector to modulate cell fate decisions, though its exact molecular mechanisms remain under investigation.
The recombinant PDRG1 protein, produced via *in vitro* expression systems (e.g., *E. coli* or mammalian cells), is a valuable tool for functional studies. It enables researchers to explore PDRG1's interactions with binding partners, such as p53 and HSP90. and its involvement in pathways like the unfolded protein response (UPR) and endoplasmic reticulum (ER) stress. Structural analyses reveal conserved α-helical and coiled-coil domains, hinting at roles in protein-protein interactions or scaffold functions.
Aberrant PDRG1 expression has been observed in cancers, including lung, liver, and colorectal tumors, where it may serve as a biomarker or therapeutic target. Recombinant PDRG1 facilitates *in vitro* assays (e.g., phosphorylation studies, binding kinetics) and *in vivo* models to dissect its dual roles in promoting or suppressing tumorigenesis, depending on cellular context. Additionally, it aids in drug screening to identify compounds modulating PDRG1 activity, with potential implications for cancer therapy. Despite progress, further research is needed to clarify its regulatory networks and therapeutic relevance.
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