| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | bgaC |
| Uniprot No | A1A3T0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1049aa |
| 氨基酸序列 | MADTAELAIVHATTASASWLTDPTVFAANRKPAHSSHRYVIGETREPKQSLDGEWKVRIEQARNVDVESAPFAAVDFEDGDFGAIEVPGHLQMAGYLKNKYVNIQYPWDGHEDPQAPNIPENNHVAIYRRRFALDAQLARTLENDGTVSLTFHGAATAIYVWLDGTFVGYGEDGFTPSEFDVTEALRNGNGNAADSPEAEHTLTVACYEYSSASWLEDQDFWRLHGLFRTVELAAQPHTHVETVQLEADYTAADTAGTADTAELNAALTLRNPADAMTIESTLRDGDGNVVWESTQACNGEIALNSGKMTNIAPWSAESPTLYTLTVRVVGHDGAIIETVTQKIGFRTFRIENGIMTINGKRIVFKGADRHEFDAKRGRAITREDMLSDVVFCKRHNINAIRTSHYPNQEYWYDLCDEYGLYLIDETNMETHGTWVANNVERPEDGIPGSRPEWEGACVDRINSMMRRDYNHPSVLIWSLGNESSAGEVFRAMYRHAHTIDPNRPVHYEGSVHMREFEDVTDIESRMYAHADEIERYLNDGSPAHTDGPKKPYISCEYMHAMGNSCGNMDEYTALERYPMYQGGFIWDFIDQAIETKLPDGTTRMCYGGDFGDRPSDYEFSGDGLLFADRTPSPKAQEVKQLYANVKIAVSVDEARITNDNLFVSTGDYRFVLRILADGKPVWSTTRRFDVAAGESASFEVDWPVDDYRSNAEELVLEVSQQLGNACDWAPAGYELAFGQCVVAGAKTTADAVDAAGAPADGTVTLGRWNAGVRGQGREALFSRTQGGMVSYTFGEREFVLRRPSITTFRPLTDNDRGAGHAFERAAWAVAGKYARCVDCAIANRGENAVEATYTYELAIPQRTKVTVRYVADTAGLVSLDVEYPGEKNGDLPTIPAFGIEWALPVEYANLRFYGAGPEETYADRRHAKLGVWSTTAGDDCAPYLLPQETGNHEDVRWAEITDDSGHGVRVKRGAGAKPFAMSLLPYSSTMLEEALHQDELPKPRHMFLRLLAAQMGVGGDDSWMSPVHEQYQLPADQPLSLNVQLKLF |
| 预测分子量 | 116,4 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BgaC重组蛋白的3篇参考文献示例(注：文献为虚构示例，仅作格式参考)：
1. **文献名称**：*Heterologous Expression and Characterization of BgaC from Bacillus subtilis in E. coli*
**作者**：Hidaka, M., et al.
**摘要**：本研究在大肠杆菌中成功表达了枯草芽孢杆菌来源的BgaC β-半乳糖苷酶，优化了诱导条件并纯化获得高活性重组蛋白，酶学分析表明其最适反应温度为40°C，pH 6.0.适用于乳糖降解。
2. **文献名称**：*Crystal Structure of Recombinant BgaC Reveals Substrate Binding Mechanism*
**作者**：Sakurai, T., et al.
**摘要**：通过X射线晶体学解析了重组BgaC的三维结构，揭示了其活性中心的关键氨基酸残基(如Glu351和Tyr503)，并阐明了底物特异性结合机制，为理性设计热稳定性突变体提供了依据。
3. **文献名称**：*Application of Recombinant BgaC in Lactose-Free Dairy Production*
**作者**：Zhang, Y., et al.
**摘要**：将重组BgaC应用于乳制品加工，证明其可高效水解牛奶中的乳糖，且在低温(4°C)下保持活性，为乳糖不耐受人群提供了新型酶解工艺。
如需真实文献，建议通过PubMed或Web of Science检索关键词“BgaC recombinant protein”、“Bacillus β-galactosidase expression”。
**Background of BgaC Recombinant Protein**
BgaC is a bacterial β-galactosidase enzyme originally identified in *Bacillus subtilis* and related species. It belongs to the glycoside hydrolase family 42 (GH42), catalyzing the hydrolysis of β-galactosidic bonds in substrates like lactose or synthetic analogs (e.g., X-gal, ONPG). This enzyme plays a role in carbon metabolism, enabling bacteria to utilize lactose as an energy source. Its robust activity, thermal stability, and broad pH tolerance make it a valuable tool in molecular biology and industrial applications.
Recombinant BgaC refers to the protein produced through genetic engineering, typically by cloning the *bgaC* gene into expression vectors (e.g., *E. coli* systems) for large-scale production. Purification tags (e.g., His-tags) are often incorporated to facilitate isolation. Unlike native forms, recombinant BgaC can be optimized for enhanced solubility, stability, or activity via mutagenesis, making it adaptable to diverse experimental or industrial needs.
In research, BgaC is widely used as a reporter enzyme. Its ability to cleave chromogenic substrates like X-gal enables visual detection in cloning (e.g., blue-white screening) or gene expression assays. In biotechnology, it aids in lactose removal in dairy products or synthesis of galacto-oligosaccharides. Additionally, BgaC serves as a model enzyme for studying protein engineering, substrate specificity, and thermostability mechanisms.
Recent studies focus on modifying BgaC for improved performance under extreme conditions or novel substrates, expanding its utility in synthetic biology and biocatalysis. Its simplicity, cost-effectiveness, and versatility continue to drive interest in both academic and industrial contexts.
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