| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HBXIP |
| Uniprot No | O43504 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-173aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMEPGAG HLDGHRAGSP SLRQALCDGS AVMFSSKERG RCTVINFVPL EAPLRSTPRS RQVTEACGGE GRAVPLGSEP EWSVGGMEAT LEQHLEDTMK NPSIVGVLCT DSQGLNLGCR GTLSDEHAGV ISVLAQQAAK LTSDPTDIPV VCLESDNGNI MIQKHDGITV AVHKMAS |
| 预测分子量 | 21 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HBXIP重组蛋白的3篇模拟参考文献及摘要概括：
1. **《HBXIP重组蛋白促进肝癌细胞增殖的分子机制研究》**
作者：李明等
摘要：该研究通过构建HBXIP重组蛋白，发现其能够激活PI3K/AKT信号通路，显著增强肝癌细胞的增殖能力，并抑制细胞凋亡。实验表明HBXIP可能通过与宿主蛋白相互作用调控肿瘤进展。
2. **《HBXIP与乙型肝炎病毒X蛋白的相互作用及其对病毒复制的影响》**
作者：王芳等
摘要：利用重组HBXIP蛋白进行体外结合实验，证实其直接结合HBV X蛋白，形成复合物并促进病毒基因组复制。研究为HBV感染的治疗提供了潜在靶点。
3. **《HBXIP重组蛋白的晶体结构解析及其功能域分析》**
作者：陈涛等
摘要：通过X射线衍射技术解析了HBXIP重组蛋白的三维结构，发现其N端结构域在结合宿主细胞因子中起关键作用。该结构信息为设计针对HBXIP的小分子抑制剂奠定了基础。
(注：以上文献为示例，实际研究中需查阅具体数据库获取真实文献。)
HBXIP (Hepatitis B X-interacting protein), initially identified as a binding partner of the hepatitis B virus X (HBx) protein, has emerged as a multifunctional regulator in cellular processes and disease pathogenesis. It is encoded by the *HBXIP* gene (also known as *LAMTOR5*) and is evolutionarily conserved across eukaryotes. Structurally, HBXIP contains a conserved N-terminal domain critical for protein interactions and a C-terminal region involved in subcellular localization.
In normal physiology, HBXIP serves as a co-factor of the mammalian Lon protease AAA+ complex, participating in mitochondrial protein quality control and metabolism regulation. However, its oncogenic potential has drawn significant attention. HBXIP overexpression is frequently observed in various cancers (e.g., breast, liver, and gastric cancers), where it promotes tumor progression by modulating cell cycle progression, inhibiting apoptosis, and enhancing glycolytic metabolism through interactions with key regulators like c-Myc and survivin.
Recombinant HBXIP protein production typically employs bacterial (e.g., *E. coli*) or mammalian expression systems, often fused with tags (His-tag, GST) for purification. Its recombinant form enables structural studies, interaction mapping (particularly with HBx in HBV-related hepatocarcinogenesis), and therapeutic target validation. Challenges in recombinant production include maintaining proper folding due to its flexible domains and preserving post-translational modifications critical for certain functions. Current research leverages HBXIP recombinant proteins to develop diagnostic biomarkers and small-molecule inhibitors targeting its oncogenic interfaces, while also exploring its role in viral replication mechanisms.
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