纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | C7orf33 |
Uniprot No | Q8WU49 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-177aa |
氨基酸序列 | MQVEVQSLSL EECPWRLPGP QCECEALLPS GARRRIDLRL SGRAVAVWVH VRGGPGQFNL SYATGRHKKP NPHQNMNRGM EFIAPVSAPT KSGAPWHFLS QGPTDAQRAV RIRPGTRMGL SSDPVVGTLS SSYLDLLTLS YKPGRTVTSS YLNVRGHEVR KLQNSVEATR ISRTDSS |
分子量 | 45.9 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C7orf33蛋白的示例性参考文献(注:文献为虚拟示例,实际研究需查询权威数据库):
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1. **文献名称**: *Expression and Purification of Recombinant Human C7orf33 in E. coli*
**作者**: Smith J. et al. (2020)
**摘要**: 本研究成功构建了人C7orf33的重组表达载体,利用大肠杆菌系统实现蛋白的可溶性表达,并通过亲和层析纯化获得高纯度蛋白。进一步的圆二色谱分析表明其具有α-螺旋主导的结构特征。
2. **文献名称**: *Functional Characterization of C7orf33 in Cell Cycle Regulation*
**作者**: Zhang Y. et al. (2019)
**摘要**: 通过RNA干扰技术敲低C7orf33表达,发现其缺失导致细胞周期G1/S期阻滞,并抑制细胞增殖。实验表明C7orf33可能通过调控Cyclin D1表达参与细胞周期进程。
3. **文献名称**: *C7orf33 Overexpression in Colorectal Cancer Tissues*
**作者**: Johnson R. et al. (2021)
**摘要**: 在结直肠癌组织样本中观察到C7orf33蛋白显著上调,且高表达与患者不良预后相关。体外实验显示,重组C7orf33可增强癌细胞迁移能力,提示其潜在促癌作用。
4. **文献名称**: *Interaction Network Analysis of C7orf33 Using Mass Spectrometry*
**作者**: Lee S. et al. (2018)
**摘要**: 通过免疫共沉淀结合质谱技术,鉴定出C7orf33与多个参与RNA加工的蛋白(如hnRNP家族成员)存在相互作用,提示其可能在转录后调控中发挥功能。
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如需真实文献,建议通过 **PubMed** 或 **Web of Science** 搜索关键词:`"C7orf33" AND ("recombinant" OR "expression" OR "function")`,并筛选近年的研究。
**Background of Recombinant Human C7orf33 Protein**
The recombinant human C7orf33 protein, encoded by the C7orf33 gene located on chromosome 7 (7p22.1), is a relatively understudied protein with emerging roles in cellular processes. Though its precise molecular function remains unclear, bioinformatics analyses suggest it may harbor structural motifs indicative of enzymatic or regulatory activity, such as putative transmembrane domains or phosphorylation sites. Current research links C7orf33 to mitochondrial function, potentially influencing energy metabolism, apoptosis, or autophagy. Studies in model organisms hint at its involvement in stress responses and cell cycle regulation, with upregulated expression observed under oxidative or hypoxic conditions.
Disease associations are poorly defined, but preliminary data implicate C7orf33 dysregulation in neurodegenerative disorders and certain cancers, possibly through interactions with pathways like mTOR or Wnt signaling. Its recombinant form is typically expressed in *E. coli* or mammalian systems for structural and functional studies, enabling antibody production and interaction partner screening. However, comprehensive mechanistic insights remain limited, necessitating further exploration of its physiological and pathological relevance. C7orf33 represents a promising yet enigmatic target for understanding cellular homeostasis and disease mechanisms.
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