纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | EPDR1 |
Uniprot No | Q9UM22 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 38-224aa |
氨基酸序列 | APR PCQAPQQWEG RQVMYQQSSG RNSRALLSYD GLNQRVRVLD ERKALIPCKR LFEYILLYKD GVMFQIDQAT KQCSKMTLTQ PWDPLDIPQN STFEDQYSIG GPQEQITVQE WSDRKSARSY ETWIGIYTVK DCYPVQETFT INYSVILSTR FFDIQLGIKD PSVFTPPSTC QMAQLEKMSE DCSW |
预测分子量 | 25,4 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EPDR1重组蛋白的假设性参考文献示例(请注意,文献信息为模拟生成,仅供参考):
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1. **文献名称**:Structural Characterization of Recombinant Human EPDR1 Protein Expressed in *E. coli*
**作者**:Chen L, Wang Y, et al.
**摘要**:本研究通过大肠杆菌表达系统成功制备了重组人源EPDR1蛋白,并利用镍柱亲和层析纯化。通过圆二色光谱和X射线晶体学分析,揭示了EPDR1的β-折叠主导结构,并发现其钙离子结合能力可能与细胞黏附功能相关。
2. **文献名称**:Functional Analysis of EPDR1 in Cancer Cell Migration via Recombinant Protein Overexpression
**作者**:Kim S, Park JH, et al.
**摘要**:通过哺乳动物细胞表达重组EPDR1蛋白,发现其过表达显著抑制乳腺癌细胞的迁移和侵袭。进一步机制研究表明,EPDR1可能通过调控Wnt/β-catenin信号通路影响肿瘤转移。
3. **文献名称**:Development of a High-Yield EPDR1 Recombinant Protein Production System Using HEK293 Cells
**作者**:Garcia R, Müller T, et al.
**摘要**:优化了HEK293细胞中EPDR1重组蛋白的分泌表达条件,获得高纯度糖基化蛋白。质谱分析确认了蛋白翻译后修饰模式,为后续功能研究和抗体开发提供了可靠材料。
4. **文献名称**:EPDR1 Recombinant Protein Binds to Laminin and Modulates Neurite Outgrowth *in vitro*
**作者**:Saito M, Tanaka K, et al.
**摘要**:体外实验表明,重组EPDR1蛋白能够结合细胞外基质成分层粘连蛋白,并促进神经元突起的生长,提示其在神经系统发育或损伤修复中的潜在作用。
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注:以上文献为模拟生成,实际研究中请通过PubMed、Google Scholar等平台检索真实发表的文章。
**Background of EPDR1 Recombinant Protein**
EPDR1 (Ependymin-Related Protein 1) is a member of the ependymin family, a group of secreted glycoproteins initially identified in teleost fish for their roles in neural plasticity and regeneration. In humans, EPDR1 is evolutionarily conserved and expressed in various tissues, including the brain, lungs, and reproductive organs. Its exact biological function remains under investigation, but studies suggest involvement in cell adhesion, differentiation, and extracellular matrix interactions. Structural analysis reveals a conserved β-sandwich fold with potential calcium-binding motifs, hinting at regulatory roles in cellular signaling.
The recombinant EPDR1 protein is engineered using biotechnology platforms, such as *E. coli* or mammalian expression systems, to ensure high purity and functionality. Researchers employ it to study EPDR1's interactions with ligands, receptors, or other proteins, particularly in contexts like cancer progression, neurodevelopment, and metabolic disorders. For instance, EPDR1 has been linked to tumorigenesis in certain cancers, where it may modulate cell migration or apoptosis. Its recombinant form enables precise in vitro and in vivo experiments, aiding in the development of diagnostic tools or therapeutic strategies targeting EPDR1-associated pathways.
Current research also explores EPDR1's potential as a biomarker due to its differential expression in pathological states. Despite gaps in mechanistic understanding, EPDR1 recombinant protein serves as a critical reagent for unraveling its physiological and pathological significance, bridging molecular biology with translational medicine.
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