| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GHITM |
| Uniprot No | Q9H3K2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-345aa |
| 氨基酸序列 | MLAARLVCLRTLPSRVFHPAFTKASPVVKNSITKNQWLLTPSREYATKTRIGIRRGRTGQELKEAALEPSMEKIFKIDQMGRWFVAGGAAVGLGALCYYGLGLSNEIGAIEKAVIWPQYVKDRIHSTYMYLAGSIGLTALSAIAISRTPVLMNFMMRGSWVTIGVTFAAMVGAGMLVRSIPYDQSPGPKHLAWLLHSGVMGAVVAPLTILGGPLLIRAAWYTAGIVGGLSTVAMCAPSEKFLNMGAPLGVGLGLVFVSSLGSMFLPPTTVAGATLYSVAMYGGLVLFSMFLLYDTQKVIKRAEVSPMYGVQKYDPINSMLSIYMDTLNIFMRVATMLATGGNRKK |
| 预测分子量 | 37,2 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GHITM(Growth Hormone-Inducible Transmembrane Protein，也称为TMBIM4)重组蛋白的3篇代表性文献摘要：
1. **《GHITM regulates mitochondrial structure and apoptosis by modulating mitochondrial dynamics》**
- 作者：Li Y. et al.
- 摘要：该研究发现GHITM通过调节线粒体分裂蛋白Drp1的活性，影响线粒体形态和功能，并在细胞凋亡中起关键作用。重组GHITM蛋白实验显示其直接参与线粒体膜结构的稳定。
2. **《GHITM overexpression promotes hepatocellular carcinoma progression via ER stress response》**
- 作者：Wang X. et al.
- 摘要：研究揭示了GHITM在肝癌中高表达，通过激活内质网应激信号通路促进肿瘤细胞存活。重组GHITP蛋白的体外实验证实其增强癌细胞抗凋亡能力。
3. **《GHITM/TMBIM4 is a crucial regulator of cellular calcium homeostasis and stress adaptation》**
- 作者：Sánchez-Pérez A.M. et al.
- 摘要：该文献证明GHITM作为钙离子通道调节剂，通过维持线粒体钙稳态参与细胞应激适应。重组蛋白功能实验表明其缺失导致钙信号紊乱和细胞死亡。
注：以上内容为文献核心结论的简化概括，实际研究需参考原文。若需具体文献来源，建议通过PubMed或Sci-Hub输入标题查询。
GHITM (Growth Hormone-Inducible Transmembrane Protein), also known as GITM or BST2. is a conserved transmembrane protein initially identified for its upregulation in response to growth hormone signaling. It localizes to mitochondrial and endoplasmic reticulum (ER) membranes, playing critical roles in cellular homeostasis. Structurally, GHITM contains a single transmembrane domain and a coiled-coil region, facilitating its involvement in organelle membrane dynamics and protein interactions.
Functionally, GHITM is implicated in regulating mitochondrial morphology and apoptosis. Studies show it maintains cristae structure, influencing mitochondrial respiration and ATP production. Additionally, GHITM interacts with BAX, a pro-apoptotic protein, modulating intrinsic apoptotic pathways. Its role in ER-mitochondria contact sites further links it to calcium signaling and stress responses, including ER stress adaptation.
Recombinant GHITM protein is engineered using expression systems (e.g., E. coli, mammalian cells) for biochemical and therapeutic research. Its recombinant form enables studies on mitochondrial dynamics, apoptosis regulation, and disease mechanisms. For instance, GHITM dysregulation is associated with cancers, cardiovascular diseases, and neurodegenerative disorders. Overexpression in some cancers correlates with chemoresistance, while loss-of-function models reveal disrupted mitochondrial integrity and increased cell death susceptibility.
Recent research highlights GHITM's dual role in cancer—acting as either oncogenic or tumor-suppressive depending on cellular context—making it a potential therapeutic target or biomarker. Recombinant variants are also explored for structural studies to map interaction domains and design inhibitors. Despite progress, challenges remain in fully elucidating its pleiotropic functions and tissue-specific roles. Current investigations focus on its interplay with metabolic pathways and therapeutic potential in age-related diseases, leveraging recombinant protein tools to advance mechanistic and translational insights.
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