| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FGA |
| Uniprot No | Q8WW76 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 36-218aa |
| 氨基酸序列 | GPRVVERHQSACKDSDWPFCSGEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVTANNLLVARVTTEETPHLKARAIKWQMRPEVKPIMKEHIAPREAMLNLALSEVSTLLLWGSLPCPPRLS |
| 预测分子量 | 25.1 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. |
以下为3篇与FGA重组蛋白相关的文献示例(注：文献信息为模拟概括，实际引用需核实原文)：
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1. **标题**：*Recombinant Human Fibrinogen Alpha Chain (FGA) Expression in E. coli and Functional Characterization*
**作者**：Smith J, et al.
**摘要**：研究报道了在大肠杆菌系统中高效表达重组人FGA蛋白的优化方法，并通过体外凝血实验验证其与天然FGA相似的纤维蛋白聚合功能。
2. **标题**：*FGA-Derived Peptides as Novel Hemostatic Agents in Trauma Models*
**作者**：Li X, et al.
**摘要**：探讨了基于FGA重组蛋白设计的多肽片段在小鼠创伤模型中的止血效果，发现其能显著缩短凝血时间并减少失血量。
3. **标题**：*Structural Analysis of FGA Mutations Associated with Congenital Fibrinogen Disorders*
**作者**：Wang Y, et al.
**摘要**：通过重组FGA突变体表达和晶体结构解析，揭示了特定氨基酸位点突变导致纤维蛋白原功能异常的分子机制。
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如需具体文献，建议通过PubMed或Web of Science检索关键词"recombinant FGA protein"或"fibrinogen alpha chain recombinant"获取最新研究。
**Background of FGA Recombinant Protein**
Fibrinogen alpha chain (FGA) is a critical component of fibrinogen, a glycoprotein essential for blood coagulation and wound healing. Native fibrinogen, synthesized in the liver, comprises three pairs of polypeptide chains (Aα, Bβ, and γ), with FGA representing the alpha subunit. During coagulation, thrombin cleaves fibrinogen to form fibrin monomers, which polymerize into clots. Beyond hemostasis, fibrinogen interacts with platelets, endothelial cells, and immune mediators, influencing inflammation, tissue repair, and disease progression.
Recombinant FGA (rFGA) is produced using genetic engineering, often in mammalian systems (e.g., CHO cells) to ensure proper post-translational modifications. This approach overcomes limitations of plasma-derived fibrinogen, such as pathogen risks and batch variability. rFGA enables precise study of fibrinogen’s structure-function relationships, particularly mutations linked to congenital fibrinogen disorders (e.g., afibrinogenemia or thrombophilia). It also serves as a scaffold in biomaterials for tissue engineering, drug delivery, and 3D cell culture due to its biocompatibility and tunable properties.
Research on rFGA advances therapeutic development, including fibrin sealants for surgery and engineered variants with enhanced clot stability or reduced immunogenicity. Additionally, it aids in modeling fibrin-related pathologies, such as thrombosis or fibrosis, offering insights into mechanistic pathways and potential drug targets. The production of rFGA underscores the convergence of biotechnology and translational medicine, addressing both clinical needs and fundamental biological questions.
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