| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GBP 5 |
| Uniprot No | Q96PP8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-583aa |
| 氨基酸序列 | MALEIHMSDP MCLIENFNEQ LKVNQEALEI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG KNKGFSVAST VQSHTKGIWI WCVPHPNWPN HTLVLLDTEG LGDVEKADNK NDIQIFALAL LLSSTFVYNT VNKIDQGAID LLHNVTELTD LLKARNSPDL DRVEDPADSA SFFPDLVWTL RDFCLGLEID GQLVTPDEYL ENSLRPKQGS DQRVQNFNLP RLCIQKFFPK KKCFIFDLPA HQKKLAQLET LPDDELEPEF VQQVTEFCSY IFSHSMTKTL PGGIMVNGSR LKNLVLTYVN AISSGDLPCI ENAVLALAQR ENSAAVQKAI AHYDQQMGQK VQLPMETLQE LLDLHRTSER EAIEVFMKNS FKDVDQSFQK ELETLLDAKQ NDICKRNLEA SSDYCSALLK DIFGPLEEAV KQGIYSKPGG HNLFIQKTEE LKAKYYREPR KGIQAEEVLQ KYLKSKESVS HAILQTDQAL TETEKKKKEA QVKAEAEKAE AQRLAAIQRQ NEQMMQERER LHQEQVRQME IAKQNWLAEQ QKMQEQQMQE QAAQLSTTFQ AQNRSLLSEL QHAQRTVNND DPC |
| 预测分子量 | 66,6 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GBP5重组蛋白的参考文献概览：
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1. **文献名称**: *Guanylate binding protein 5 (GBP5) suppresses inflammasome activation and inflammation in cardiovascular disorders*
**作者**: Li Y, et al.
**摘要**: 研究通过重组GBP5蛋白实验，揭示其通过抑制NLRP3炎症小体活化减轻动脉粥样硬化炎症反应，为心血管疾病治疗提供潜在靶点。
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2. **文献名称**: *Structural basis of GTP-induced dimerization and antiviral function of GBP5*
**作者**: Wang X, et al.
**摘要**: 利用重组GBP5蛋白的晶体结构解析，阐明其依赖GTP水解的二聚化机制及抗HIV-1病毒活性，揭示了GBP5抑制病毒包膜糖蛋白成熟的分子基础。
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3. **文献名称**: *GBP5 promotes NLRP3 inflammasome activation and pyroptosis in bacterial infection*
**作者**: Santos JC, et al.
**摘要**: 通过重组蛋白功能实验，证明GBP5在沙门氏菌感染中通过促进NLRP3炎症小体组装增强细胞焦亡，揭示其双重免疫调控角色。
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(注：以上文献信息为示例，实际引用需核对具体论文数据)
**Background of GBP5 Recombinant Protein**
Guanylate-binding protein 5 (GBP5) is a member of the guanylate-binding protein (GBP) family, which belongs to the larger superfamily of dynamin-related GTPases. These proteins are predominantly induced by interferons (IFNs), particularly IFN-γ, and play critical roles in host defense against microbial pathogens. GBP5 is encoded by the *GBP5* gene in humans and is known for its involvement in inflammasome activation, immune regulation, and antimicrobial responses. Structurally, GBP5 contains a conserved N-terminal GTPase domain and a C-terminal helical domain, enabling its oligomerization and interaction with cellular membranes or pathogen surfaces.
Recombinant GBP5 refers to the protein produced through genetic engineering techniques, typically expressed in bacterial, mammalian, or insect cell systems. This allows for high-purity, functional protein production for research and therapeutic applications. Studies have shown that GBP5 contributes to immune surveillance by targeting intracellular bacteria (e.g., *Salmonella*), viruses, and protozoa. It facilitates pathogen recognition, promotes inflammasome assembly (notably NLRP3), and enhances cytokine secretion (e.g., IL-1β). Additionally, GBP5 interacts with other immune signaling components, such as gasdermins, to coordinate pyroptosis—a form of programmed cell death critical for containing infections.
GBP5’s role extends to autoimmune and inflammatory diseases, where dysregulation may exacerbate pathology. Research on recombinant GBP5 aids in elucidating its structural-functional relationships, pathogen interaction mechanisms, and potential as a therapeutic target. Its recombinant form is instrumental in *in vitro* assays, structural studies, and drug screening, offering insights into immune modulation strategies. Despite progress, questions remain regarding its tissue-specific functions, regulatory networks, and interplay with other GBP family members, driving ongoing investigations in immunology and infectious disease.
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