| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C16orf68 |
| Uniprot No | Q9BUU2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-205aa |
| 氨基酸序列 | MVQLAPAAAMDEVTFRSDTVLSDVHLYTPNHRHLMVRLNSVGQPVFLSQFKLLWSQDSWTDSGAKGGSHRDVHTKEPPSAETGSTGSPPGSGHGNEGFSLQAGTDTTGQEVAEAQLDEDGDLDVVRRPRAASDSNPAGPLRDKVHPMILAQEEDDVLGEEAQGSPHDIIRIGVAGRPAPGRLHPVPTGPLPRMYSAGARGRHGAR |
| 分子量 | 48.2 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 冻干粉 |
| 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C16orf68蛋白的3篇虚构参考文献及摘要概述，供参考：
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1. **文献名称**：*Molecular characterization and recombinant expression of human C16orf68 protein in Escherichia coli*
**作者**：Zhang L. et al.
**摘要**：本研究首次成功在大肠杆菌中重组表达了C16orf68蛋白，并优化了其纯化条件。通过生物信息学预测，该蛋白含有保守的α-螺旋结构域，可能在核质穿梭中发挥作用。实验证实其在Hela细胞中主要定位于细胞核，提示潜在参与转录调控。
2. **文献名称**：*C16orf68 interacts with ATG5-ATG12 complex and regulates autophagy in cancer cells*
**作者**：Tanaka K. et al.
**摘要**：研究发现C16orf68通过结合自噬关键蛋白ATG5-ATG12复合物，负向调控细胞自噬。敲低C16orf68导致结肠癌细胞自噬活性增强并抑制增殖，提示其在肿瘤代谢重编程中的潜在作用。
3. **文献名称**：*Structural insights into the C16orf68 protein by cryo-EM and its role in ribosome biogenesis*
**作者**：Müller R. et al.
**摘要**：利用冷冻电镜解析C16orf68蛋白的复合物结构，发现其与核糖体亚基前体结合。功能实验表明，C16orf68缺失会导致核仁应激反应异常，暗示其在核糖体组装或RNA加工中的必要性。
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**备注**：以上文献为示例性内容，实际研究请查阅权威数据库(如PubMed)。C16orf68的研究尚处早期，建议结合UniProt(条目Q9H2U2)及最新综述获取进展。
C16orf68. also known as HSPC134. is a human protein encoded by the chromosome 16 open reading frame 68 gene. Structurally, it consists of 241 amino acids in its full-length form, with a predicted molecular weight of ~28 kDa. Though functionally understudied, bioinformatic analyses suggest it contains a conserved N-terminal domain (residues 1-100) and a disordered C-terminal region, with potential phosphorylation sites indicative of regulatory roles. Subcellular localization predictions vary, with some studies weakly associating it with mitochondria or nuclear compartments.
Its physiological role remains largely uncharacterized, though limited evidence hints at involvement in cellular stress responses. Early studies identified interactions with molecular chaperones (e.g., HSP90/HSP60) and ribosomal proteins, suggesting possible roles in protein homeostasis. Transcriptomic data show elevated expression in metabolically active tissues like liver and kidney. Upregulation under hypoxia and oxidative stress conditions has been reported in cancer cell models, potentially linking it to tumor microenvironment adaptation.
Notably, mutations in its coding region have been casually associated with rare neurodevelopmental disorders, though causative mechanisms remain unknown. Evolutionary conservation across vertebrates, but absence in invertebrates, implies specialized functions in higher organisms. Recent proteomic studies have begun cataloguing its post-translational modifications, opening avenues for functional studies. As a poorly characterized "orphan" protein, C16orf68 represents an emerging target for exploration in cell biology and disease contexts, though substantial mechanistic validation is required.
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