纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FLJ39155 |
Uniprot No | Q63HQ2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-152aa |
氨基酸序列 | MRFKTTAKDGLLLWRGDSPMRPNSDFISLGLRDGALVFSYNLGSGVASIMVNGSFNDGRWHRVKAVRDGQSGKITVDDYGARTGKSPGMMRQLNINGALYVGGMKEIALHTNRQYMRGLVGCISHFTLSTDYHISLVEDAVDGKNINTCGAK |
分子量 | 43 kDa |
蛋白标签 | GST-tag at N-terminal |
缓冲液 | 0 |
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. |
以下是关于重组人FLJ39155蛋白的模拟参考文献示例(请注意,以下内容基于假设性研究,非真实文献):
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1. **文献名称**:*Expression and Functional Analysis of Recombinant Human FLJ39155 in Hepatocellular Carcinoma*
**作者**:Zhang, L. et al.
**摘要**:本研究成功在大肠杆菌中表达并纯化了重组人FLJ39155蛋白,发现其在高表达的肝癌细胞中显著促进细胞增殖并抑制凋亡,提示其可能作为肝细胞癌的潜在治疗靶点。
2. **文献名称**:*Recombinant FLJ39155 Protein Enhances Cellular Migration via PI3K/AKT Signaling Pathway*
**作者**:Wang, Y. & Chen, H.
**摘要**:通过体外实验证明,重组人FLJ39155蛋白通过激活PI3K/AKT通路增强乳腺癌细胞的迁移和侵袭能力,可能参与肿瘤转移调控。
3. **文献名称**:*Structural Characterization and Enzymatic Activity of Recombinant FLJ39155*
**作者**:Kim, S. et al.
**摘要**:首次报道了FLJ39155的重组表达策略及晶体结构,发现其具有非典型丝氨酸水解酶活性,为后续功能研究和药物开发奠定基础。
4. **文献名称**:*FLJ39155 as a Novel Biomarker in Colorectal Cancer: Insights from Recombinant Protein-Based Assays*
**作者**:Müller, R. et al.
**摘要**:利用重组人FLJ39155蛋白开发ELISA检测方法,发现其在结直肠癌患者血清中高表达,可能作为诊断或预后标志物。
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**备注**:以上文献为示例性内容,实际研究中请通过**PubMed**、**Google Scholar**等平台检索真实文献(可尝试关键词:FLJ39155 protein, recombinant FLJ39155. CXorf43/C1orf123等别称)。部分研究可能以基因或别名形式发表,建议结合基因数据库(如NCBI Gene, UniProt)确认最新进展。
Recombinant human FLJ39155 protein is a genetically engineered protein derived from the FLJ39155 gene, which encodes a poorly characterized protein in humans. Initially identified through cDNA sequencing projects, FLJ39155 remains understudied, with limited functional data available. Bioinformatic analyses suggest it may contain conserved structural motifs, such as transmembrane domains or enzymatic regions, hinting at potential roles in cellular signaling, metabolism, or membrane-associated processes. However, its exact biological function, interacting partners, and pathways remain elusive due to scarce experimental validation.
The production of recombinant FLJ39155 typically involves cloning its coding sequence into expression systems like *E. coli* or mammalian cells, followed by purification for *in vitro* studies. This protein is often utilized as a tool to investigate its biochemical properties, generate antibodies, or explore its role in disease contexts through functional assays. Its recombinant form enables researchers to probe its structure, post-translational modifications, and potential involvement in pathologies like cancer or metabolic disorders. Despite its enigmatic nature, FLJ39155 represents a target for exploratory research aimed at expanding the catalog of functionally annotated human proteins, bridging gaps in our understanding of cellular mechanisms and disease biology. Further studies are essential to unravel its physiological significance.
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