| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IGIP |
| Uniprot No | A6NJ69 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-53aa |
| 氨基酸序列 | KSPCGNQANVLCISRLEFVQYQS |
| 预测分子量 | 56.6 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篇关于IGIP(Immunoglobulin-binding Protein)重组蛋白的示例性文献(内容为模拟，仅供参考)：
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1. **文献名称**: *Cloning and Functional Characterization of Recombinant IGIP in E. coli*
**作者**: Zhang L. et al.
**摘要**: 本研究成功克隆并表达了IGIP基因的重组蛋白，利用大肠杆菌表达系统获得高纯度产物。实验证实重组IGIP能够特异性结合IgG的Fc段，并增强巨噬细胞的吞噬活性，为其在免疫治疗中的应用提供依据。
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2. **文献名称**: *Structural Analysis of IGIP Reveals Its Role in Pathogen Immune Evasion*
**作者**: Müller R. et al.
**摘要**: 通过X射线晶体学解析了重组IGIP的三维结构，发现其具有独特的抗原结合域。功能实验表明，病原体分泌的IGIP可通过干扰抗体介导的中和作用，促进细菌逃逸宿主免疫应答。
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3. **文献名称**: *Therapeutic Potential of Recombinant IGIP in Autoimmune Disease Models*
**作者**: Tanaka K. et al.
**摘要**: 在小鼠类风湿性关节炎模型中，注射重组IGIP显著降低了促炎细胞因子(如TNF-α、IL-6)水平，并缓解关节肿胀，提示其作为免疫调节剂的潜在价值。
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**备注**：以上文献为示例，实际研究需通过学术数据库(如PubMed、Web of Science)检索真实发表的文章。
**Background of IGIP Recombinant Protein**
IGIP (Immunoglobulin G-binding Protein) recombinant protein is a bioengineered molecule derived from natural proteins that interact with immunoglobulins, particularly IgG antibodies. Originally identified in pathogenic bacteria like *Streptococcus*, IGIP evolved as a virulence factor to evade host immune responses by binding to IgG’s Fc region, interfering with opsonization and phagocytosis. This interaction inspired its adaptation for biotechnological and therapeutic applications.
Recombinant IGIP is produced using genetic engineering techniques, where the IGIP gene is cloned into expression systems (e.g., *E. coli*, yeast, or mammalian cells) to generate purified, functional proteins. Its structure typically retains critical domains for IgG binding, ensuring biological activity. Advances in protein engineering have enabled modifications to enhance stability, specificity, or fusion with other functional domains (e.g., tags for detection or therapeutic payloads).
In research, IGIP recombinant proteins serve as tools to study immune evasion mechanisms, antibody-protein interactions, and immune modulation. Therapeutically, they are explored for applications in autoimmune diseases or inflammatory disorders by neutralizing pathogenic antibodies or modulating immune complexes. Additionally, IGIP-based platforms are investigated for antibody purification in biomanufacturing due to their high affinity for IgG.
Challenges include optimizing production yields, minimizing aggregation, and ensuring functional consistency. Ongoing studies focus on structure-function relationships and engineering IGIP variants with tailored binding properties. As a versatile molecule bridging microbiology, immunology, and biotechnology, IGIP recombinant protein continues to offer promising avenues for both basic science and applied medical innovations.
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