| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FGG |
| Uniprot No | P02679 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-453aa |
| 氨基酸序列 | YVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL |
| 预测分子量 | 55.9 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FGG重组蛋白的3篇参考文献示例(注：文献为模拟示例，非真实存在)：
1. **文献名称**：Expression and functional characterization of recombinant human fibrinogen gamma-chain (FGG) in mammalian cells
**作者**：Smith JL, et al.
**摘要**：本研究报道了利用HEK293细胞高效表达重组人FGG蛋白的方法，并验证其与天然FGG在促进血小板聚集和纤维蛋白形成中的等效生物活性。
2. **文献名称**：Structural analysis of FGG recombinant protein mutants in thrombosis models
**作者**：Wang H, et al.
**摘要**：通过基因工程技术构建了FGG的多个点突变体，解析其三维结构变化对凝血功能的影响，为抗血栓药物靶点筛选提供新思路。
3. **文献名称**：Large-scale production of bioactive FGG protein using Pichia pastoris system
**作者**：Kim S, et al.
**摘要**：开发了基于毕赤酵母的重组FGG规模化生产工艺，产量达2.8 g/L，产物经质谱验证具有正确糖基化修饰，适用于体外诊断试剂开发。
(提示：实际文献检索建议使用PubMed/Google Scholar，以"recombinant fibrinogen gamma chain"或"FGG protein expression"为关键词查询最新研究)
**Background of FGG Recombinant Protein**
Fibrinogen gamma chain (FGG) is a critical component of fibrinogen, a large glycoprotein complex essential for blood clotting. Native fibrinogen consists of three pairs of polypeptide chains (Aα, Bβ, and γ), synthesized primarily in hepatocytes. During coagulation, thrombin cleaves fibrinogen to form fibrin monomers, which polymerize into clots. The γ-chain, encoded by the *FGG* gene, plays a pivotal role in clot stability, platelet aggregation, and wound healing.
Recombinant FGG protein is engineered using genetic engineering techniques, often expressed in heterologous systems like *E. coli*, yeast, or mammalian cells (e.g., HEK293 or CHO cells). This approach allows large-scale production of purified FGG with consistent quality, circumventing risks associated with plasma-derived fibrinogen, such as pathogen contamination or batch variability. Recombinant FGG retains functional domains, including binding sites for thrombin, fibrin(ogen) receptors, and crosslinking regions critical for clot formation.
Research on recombinant FGG focuses on understanding fibrinogen’s role in hemostasis, thrombosis, and inflammation. It is also used to develop fibrin-based biomaterials for wound healing, surgical adhesives, or drug delivery systems. Additionally, recombinant FGG aids in studying fibrinogen-related disorders, such as dysfibrinogenemia or hypofibrinogenemia, and in screening therapeutics targeting clot formation or dissolution.
The production of recombinant FGG enables customization, such as introducing mutations to study structure-function relationships or engineering isoforms with enhanced stability or reduced immunogenicity. These advancements highlight its potential in translational medicine and biopharmaceutical applications.
×
