| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | pgaB |
| Uniprot No | P75906 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-672aa |
| 氨基酸序列 | CISQSRTSFIPPQDRESLLAEQPWPHNGFVAISWHNVEDEAADQRFMSVRTSALREQFAWLRENGYQPVSIAQIREAHRGGKPLPEKAVVLTFDDGYQSFYTRVFPILQAFQWPAVWAPVGSWVDTPADKQVKFGDELVDREYFATWQQVREVARSRLVELASHTWNSHYGIQANATGSLLPVYVNRAYFTDHARYETAAEYRERIRLDAVKMTEYLRTKVEVNPHVFVWPYGEANGIAIEELKKLGYDMFFTLESGLANASQLDSIPRVLIANNPSLKEFAQQIITVQEKSPQRIMHIDLDYVYDENLQQMDRNIDVLIQRVKDMQISTVYLQAFADPDGDGLVKEVWFPNRLLPMKADIFSRVAWQLRTRSGVNIYAWMPVLSWDLDPTLTRVKYLPTGEKKAQIHPEQYHRLSPFDDRVRAQVGMLYEDLAGHAAFDGILFHDDALLSDYEDASAPAITAYQQAGFSGSLSEIRQNPEQFKQWARFKSRALTDFTLELSARVKAIRGPHIKTARNIFALPVIQPESEAWFAQNYADFLKSYDWTAIMAMPYLEGVAEKSADQWLIQLTNQIKNIPQAKDKSILELQAQNWQKNGQHQAISSQQLAHWMSLLQLNGVKNYGYYPDNFLHNQPEIDLIRPEFSTAWYPKND |
| 预测分子量 | 82.6 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. |
以下是关于PgaB重组蛋白的3篇模拟参考文献(内容基于常见研究方向整合，供参考)：
1. **文献名称**：*"Characterization of PgaB as a deacetylase in poly-β-1.6-N-acetyl-D-glucosamine synthesis in Escherichia coli"*
**作者**：Wang, X., Preston, J.F., Romeo, T.
**摘要**：研究阐明了PgaB在大肠杆菌生物膜基质多糖PNAG合成中的脱乙酰酶功能，通过重组表达纯化PgaB蛋白，证实其修饰多糖乙酰化程度以调控生物膜稳定性。
2. **文献名称**：*"Structural and functional analysis of PgaB in bacterial biofilm formation"*
**作者**：Little, D.J., Poloczek, J., Whitney, J.C.
**摘要**：通过X射线晶体学解析重组PgaB蛋白的结构，揭示其与多糖底物结合的活性位点，并证明其与PgaA协同作用对PNAG的修饰至关重要。
3. **文献名称**：*"Recombinant production and enzymatic activity of PgaB from Acinetobacter baumannii"*
**作者**：Gohl, O., Friedrich, A., Hübner, N.
**摘要**：报道了鲍曼不动杆菌PgaB的重组表达及纯化，体外实验证明其具有脱乙酰酶和糖苷水解酶双功能活性，影响病原菌的毒力和生物膜形成。
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注：以上文献为示例性质，实际引用需根据具体研究通过PubMed或Web of Science检索真实文献。
**Background of PGA Recombinant Protein**
The pgaB gene encodes a key enzyme involved in the biosynthesis of poly-γ-glutamic acid (PGA), a natural biopolymer produced by various *Bacillus* species. PGA is renowned for its biocompatibility, biodegradability, and non-toxic properties, making it valuable in biomedical, agricultural, and industrial applications, such as drug delivery, hydrogels, and wastewater treatment. However, native PGA production is often limited by low yields and structural heterogeneity, prompting interest in recombinant protein strategies to optimize its synthesis and modification.
The pgaB protein functions as a γ-glutamyl hydrolase or deacetylase, playing a critical role in modulating the molecular weight and acetylation state of PGA. These structural features directly influence its physicochemical properties, including viscosity, solubility, and stability. Recombinant pgaB proteins are engineered through heterologous expression systems, typically in *Escherichia coli*, to achieve high-purity, functional enzymes for *in vitro* PGA modification. This approach allows precise control over enzymatic activity, enabling tailored PGA variants with enhanced performance for specific applications.
Recent studies have focused on elucidating pgaB's structure-function relationships, including its catalytic mechanism and substrate specificity, using X-ray crystallography and site-directed mutagenesis. These insights facilitate the rational design of engineered pgaB variants with improved stability or altered activity. Additionally, recombinant pgaB is utilized in synthetic biology platforms to streamline PGA production in non-native hosts, reducing reliance on pathogenic *Bacillus* strains.
Overall, recombinant pgaB represents a pivotal tool in advancing PGA-based technologies, bridging gaps between biopolymer research and industrial scalability. Ongoing efforts aim to harness its enzymatic versatility for sustainable material synthesis and precision biomedicine.
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