| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | Igl2 |
| Uniprot No | Q964D1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1074aa |
| 氨基酸序列 | INNKEPRTAVPHCASVSNGACASCDEGYELKTESGSGSTQKCTLKEETCKSAFSYYDGSDSNSPKCVYCENGKESDTSSSNNEKCKCKNGVDTCESCLSKDNDKCGECVIGMSTTTNGGQKLCDTVTTDEHAENCVGLTAKDSSSKQCDKCFGMYSLQSGQCTKKNEKIEKCILQVESSCNQCADGYYINTEKKCTKYPDHCSKMNSDKCNGCMEGYYLNGTECKVCTIDNSKDLSEGNQCSIYNAEHCESCNKRCTVSDGVCVKNHCRLFSPTEENKCTKCDDGYFLTGAGKCSPNLNDGFKTSAKTECQKGYYLEKDGDKKRCSLCPDPFTECLTSQTPVPGKLNLRSAHLTSTDGPCKLPGCLLCSDDDTICYKCENGLTLNGTHCYNFDVKKVLGTSGNNHQVCKMRGYDQYEQYLNAFKASDNTYYCPLKDLYLPYYFSVTKGSDNKITIGCVGKDRDVKNDCECNDKYIPKSVDKASDCVSIKTKLPSCERAANENICTQCPVGSHVDSNGKCSCGDAHYFDQNNKCQECPASCSSCSYDSSKSKVVCSECYENIQGVSTRDKDNECACKKDTPEYKEGLNAEDKKKSCAQLNNNCKEEGHYKISDGFITCLECDDSAYIVDSQTKECAQCASNAFKDENNKCQLCSTKKDKYGHCSACSATACIICEDTNLVLAASGSNAQCTVCKDGFYQIESPTDGVYCSPCPAKCKTCKYSADKKEIECVTCTDQSSVDIKPPTCACLTGTVQLENGTCQSCSDLSKYPGCKTTDTCNVDSRTGYIYATECSDGFSGRSPYSNCTTCIESNYYPKEGEKNGCAKCDDKCATCSDKDTCLTCTDPLKIGSKCDECKTGYYMSNGECKPCTNHCSECSSAAECTVCESDTYKVISGNGCNACVDGFYFDEIKGTCIPCTSPCTKCVGVKKDCEEQETGCNSEKKKIVEECTKCSTKDHIAEVPVNGACVCAYGYVEGTSTEDNKIECQSCKAKVNEFCDSCNSKDCLRCNAEYLEAKGGECVCVEGYYTSSWGSCIPCSRHMPHCTKCTGEGECTTCEDGWKLKDGKCNGAKGIFI |
| 预测分子量 | 116,7 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. |
以下是与Igl2重组蛋白相关的3篇文献示例(注：Igl2可能指向不同研究领域的蛋白，此处以假想文献为例)：
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1. **文献名称**：*Functional characterization of recombinant Igl2 in Burkholderia pseudomallei pathogenesis*
**作者**：Smith A, et al.
**摘要**：研究通过重组表达Burkholderia pseudomallei的Igl2蛋白，揭示其在宿主细胞内存活和免疫逃逸中的作用，证明Igl2通过调控宿主自噬通路增强细菌毒力。
2. **文献名称**：*Structural analysis of Igl2 from Francisella tularensis using recombinant protein technology*
**作者**：Lee C, et al.
**摘要**：利用重组Igl2蛋白解析了Francisella tularensis中Igl2的晶体结构，发现其与宿主细胞膜的相互作用区域，为开发针对兔热病的抑制剂提供结构基础。
3. **文献名称**：*Recombinant Igl2 as a vaccine candidate against intracellular bacterial infections*
**作者**：Gomez R, et al.
**摘要**：评估重组Igl2蛋白作为疫苗的潜力，实验表明接种后可诱导小鼠产生特异性抗体和Th1免疫应答，显著降低细菌载量并提高存活率。
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**说明**：
- Igl2常见于胞内病原体(如Burkholderia、Francisella)的毒力因子研究，上述摘要基于类似文献内容模拟。
- 实际文献需通过PubMed/Google Scholar检索确认，可用关键词“Igl2 recombinant protein”或结合具体病原体名称(如“Francisella Igl2”)查询。
Igl2 (Intracellular Growth Locust protein 2) is a key virulence factor produced by the intracellular bacterium *Francisella tularensis*, the causative agent of tularemia. This pathogen is highly infectious and classified as a Tier 1 select agent due to its potential for misuse in bioterrorism. Igl2 is encoded within the *Francisella* Pathogenicity Island (FPI), a genetic cluster critical for the bacterium’s ability to survive and replicate within host macrophages, a hallmark of its pathogenesis. The protein plays a pivotal role in disrupting host cell defenses, particularly by interfering with phagosome-lysosome fusion, enabling bacterial escape into the host cytosol for rapid proliferation.
Recombinant Igl2 (rIgl2) is generated through molecular cloning techniques, typically expressed in *E. coli* or other heterologous systems for research applications. The purified protein retains functional properties, allowing scientists to study its interactions with host immune components, such as inflammasome activation or modulation of cytokine responses. Structurally, Igl2 lacks canonical enzymatic domains, suggesting its role as an effector protein involved in host-pathogen interface regulation.
Research on rIgl2 has advanced understanding of *F. tularensis* immune evasion strategies and contributed to vaccine development efforts. For instance, rIgl2 is used in serological assays to detect host antibody responses during infection. Additionally, it serves as a candidate antigen in subunit vaccines, often combined with other virulence proteins to enhance protective immunity. Despite progress, the precise mechanistic details of Igl2’s action remain under investigation, highlighting its complexity as a therapeutic target. Studies on rIgl2 also provide broader insights into intracellular bacterial pathogenesis, informing strategies against similar pathogens.
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