| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AK2 |
| Uniprot No | P54819 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-239aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAPSVPAAEP EYPKGIRAVL LGPPGAGKGT QAPRLAENFC VCHLATGDML RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG FPRTVRQAEM LDDLMEKRKE KLDSVIEFSI PDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI |
| 预测分子量 | 29 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AK2(腺苷酸激酶2)重组蛋白研究的示例参考文献(部分为模拟内容，供参考)：
1. **标题**：Adenylate Kinase 2 Modulates Mitochondrial Energy Homeostasis in Cancer Cells
**作者**：Smith J, et al.
**摘要**：研究揭示了重组AK2蛋白在癌细胞线粒体能量代谢中的作用，通过调控ATP/AMP平衡影响细胞增殖和凋亡，为癌症治疗提供潜在靶点。
2. **标题**：Expression and Functional Characterization of Recombinant Human AK2 in Retroviral Disease Models
**作者**：Li X, et al.
**摘要**：报道了人源重组AK2蛋白的表达与纯化方法，并验证其在网状发育不全(一种AK2缺陷相关疾病)模型中的功能恢复作用。
3. **标题**：Structural Insights into AK2 Deficiency Using Recombinant Protein Mutagenesis
**作者**：Wang Y, et al.
**摘要**：通过重组AK2蛋白的定点突变实验，解析其结构-功能关系，阐明AK2突变导致免疫缺陷疾病的分子机制。
4. **标题**：AK2 Recombinant Protein Enhances Mitochondrial Apoptosis in Neurodegenerative Disorders
**作者**：Garcia R, et al.
**摘要**：证明重组AK2蛋白通过激活线粒体凋亡通路，在神经退行性疾病模型中减少神经元损伤，提示其潜在治疗价值。
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**注意**：以上文献为示例性内容，建议通过PubMed、Web of Science等平台检索真实文献(关键词：AK2 recombinant protein, adenylate kinase 2 expression)。如需具体文献，可提供研究方向(如疾病机制、蛋白纯化等)以便进一步筛选。
**Background of AK2 Recombinant Protein**
Adenylate kinase 2 (AK2), a member of the adenylate kinase family, is a critical enzyme involved in cellular energy metabolism. It catalyzes the reversible transfer of phosphate groups between adenosine nucleotides (ATP, ADP, and AMP), maintaining energy homeostasis and supporting processes like cell proliferation, differentiation, and apoptosis. AK2 is predominantly localized in the mitochondrial intermembrane space and cytosol, where it plays a role in mitochondrial function and stress responses.
The recombinant AK2 protein is engineered using genetic recombination technology, enabling its production in heterologous expression systems (e.g., *E. coli* or mammalian cells*)*. This approach ensures high purity and scalability for research and therapeutic applications. AK2 has garnered attention due to its association with human diseases. Mutations in the *AK2* gene are linked to rare genetic disorders such as reticular dysgenesis (RD), a severe immunodeficiency syndrome, and certain forms of mitochondrial dysfunction. Additionally, AK2 is implicated in apoptotic pathways, interacting with proteins like FADD and participating in caspase activation.
Recombinant AK2 serves as a vital tool for studying mitochondrial bioenergetics, immune cell development, and disease mechanisms. Its applications extend to drug discovery, particularly in targeting metabolic disorders and cancers characterized by dysregulated apoptosis. Structural and functional studies using recombinant AK2 have provided insights into its catalytic mechanism and interaction networks, aiding the design of small-molecule modulators.
In production, AK2 recombinant protein is typically purified via affinity tags (e.g., His-tag) and validated through enzymatic assays and binding studies. Its stability and activity are optimized for *in vitro* and *in vivo* models, reinforcing its utility in both basic research and translational medicine. Overall, AK2 recombinant protein bridges molecular biology and clinical insights, offering a versatile platform to explore cellular energetics and therapeutic interventions.
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