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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | int |
| Uniprot No | P04426 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-370aa |
| 氨基酸序列 | ANSSGRWWGIVNIASSTNLLTDSKSLQLVLEPSLQLLSRKQRRLIRQNPGILHSVSGGLQSAVRECKWQFRNRRWNCPTAPGPHLFGKIVNRGCRETAFIFAITSAGVTHSVARSCSEGSIESCTCDYRRRGPGGPDWHWGGCSDNIDFGRLFGREFVDSGEKGRDLRFLMNLHNNEAGRTTVFSEMRQECKCHGMSGSCTVRTCWMRLPTLRAVGDVLRDRFDGASRVLYGNRGSNRASRAELLRLEPEDPAHKPPSPHDLVYFEKSPNFCTYSGRLGTAGTAGRACNSSSPALDGCELLCCGRGHRTRTQRVTERCNCTFHWCCHVSCRNCTHTRVLHECL |
| 预测分子量 | 45.8 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3篇与 **int重组蛋白**(整合酶相关)相关的研究文献，供参考：
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1. **文献名称**：*Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases*
**作者**：Hickman, A.B., et al.
**摘要**：该研究解析了HIV-1整合酶催化核心域(重组表达)的晶体结构，揭示了其与其他多核苷酸转移酶(如转座酶)的结构相似性，为理解病毒DNA整合机制及抑制剂设计提供依据。
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2. **文献名称**：*Purification and characterization of recombinant human immunodeficiency virus type 1 integrase*
**作者**：Sherman, P.A., & Fyfe, J.A.
**摘要**：报道了通过大肠杆菌重组表达系统高效制备HIV-1整合酶的方法，并对其酶活性和金属离子依赖性进行功能验证，为后续抗病毒药物筛选奠定基础。
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3. **文献名称**：*Mechanistic flexibility of retroviral integrases*
**作者**：Chiu, T.K., & Davies, D.R.
**摘要**：通过重组表达的逆转录病毒整合酶(包括HIV和PFV)对比研究，揭示了整合酶催化DNA链转移反应的多步骤机制及结构动态变化，强调了其在基因编辑技术中的潜在应用。
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4. **文献名称**：*Functional analysis of the integrase protein of human immunodeficiency virus type 1 using recombinant mutants*
**作者**：Engelman, A., et al.
**摘要**：通过构建重组整合酶突变体，系统研究了其N端、催化核心及C端结构域的功能差异，阐明了各区域在病毒DNA结合与整合过程中的协同作用。
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**注**：以上文献均围绕整合酶(int重组蛋白)的重组表达、结构解析及功能机制展开，涉及抗病毒药物开发或基因编辑研究领域。如需具体期刊信息或发表年份，可进一步补充关键词检索。
**Background of Integrase (INT) Recombinant Proteins**
Integrase (INT) recombinant proteins are engineered molecules derived from integrase enzymes, which play critical roles in mediating the integration of viral genetic material into host genomes. Initially studied in retroviruses like HIV-1. integrases catalyze the insertion of viral DNA into host DNA, a key step in viral replication. This unique function has made integrases a focal point in virology, drug development, and genetic engineering.
The development of recombinant integrase proteins emerged with advancements in molecular cloning and protein expression technologies. By isolating and modifying the integrase gene, researchers produce these proteins in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells*), enabling large-scale purification and functional studies. Recombinant INT proteins retain enzymatic activity, allowing *in vitro* studies of integration mechanisms, substrate specificity, and inhibition.
In drug discovery, recombinant integrases serve as targets for antiviral agents. HIV integrase inhibitors, such as raltegravir, were developed using *in vitro* assays with recombinant proteins, highlighting their translational value. Beyond virology, integrase-based recombinant tools are explored in genetic engineering. For instance, phage integrases are adapted for site-specific gene insertion in synthetic biology, offering precision over traditional methods like CRISPR in certain contexts.
Challenges in working with INT recombinant proteins include maintaining structural stability and activity, as integrases often require chaperones or specific conditions for proper folding. Additionally, understanding their interactions with host factors remains complex. Despite this, ongoing research aims to expand their applications, including gene therapy and biotechnology.
Overall, integrase recombinant proteins bridge fundamental virology and applied sciences, driving innovations in medicine and genetic manipulation. Their study continues to uncover novel mechanisms and therapeutic strategies, underscoring their importance in molecular research.
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