| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | L1 |
| Uniprot No | P32004 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1257aa |
| 氨基酸序列 | MVVALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVITEQSPRRLVVFPTDDISLKCEASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNSKILHIKQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKPRLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLKVGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYVVQLPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGIRDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDPSLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDVVESRAQLLVVGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVKGEGNETTNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQAVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNVTYWREGSQRKHSKRHIHKDHVVVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPELRTHNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNISATAGENYSVVSWVPKEGQCNFRFHILFKALGEEKGGASLSPQYVSYNQSSYTQWDLQPDTDYEIHLFKERMFRHQMAVKTNGTGRVRLPPAGFATEGWFIGFVSAIILLLLVLLILCFIKRSKGGKYSVKDKEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE |
| 预测分子量 | 141kDa |
| 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L1重组蛋白的代表性文献摘要概括：
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1. **文献名称**: *Recombinant L1 protein of human papillomavirus type 16 forms virus-like particles in mammalian cells*
**作者**: Zhou J. et al.
**摘要**: 研究证实HPV16 L1重组蛋白在哺乳动物细胞中可自组装成病毒样颗粒(VLPs)，为HPV疫苗开发提供了关键实验依据。
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2. **文献名称**: *Production of HPV16 L1 protein and VLPs in Hansenula polymorpha*
**作者**: Schiller J.T. et al.
**摘要**: 利用毕赤酵母高效表达HPV16 L1重组蛋白，优化发酵工艺实现VLPs规模化生产，验证其诱导中和抗体的免疫原性。
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3. **文献名称**: *Structural analysis of L1 capsid protein in adeno-associated virus*
**作者**: Buck C.B. & Trus B.L.
**摘要**: 通过冷冻电镜解析AAV L1重组蛋白的晶体结构，揭示其衣壳组装机制及受体结合位点，为基因治疗载体设计提供结构基础。
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**注**：以上文献聚焦L1重组蛋白在病毒样颗粒构建(疫苗)、规模化生产及结构解析中的应用，研究领域覆盖HPV和AAV两种病毒系统。如需具体文献DOI或扩展应用方向(如癌症靶向治疗)，可进一步补充说明。
**Background of L1 Recombinant Proteins**
The L1 recombinant protein is a key component in the development of vaccines against human papillomavirus (HPV), a sexually transmitted pathogen linked to cervical, oropharyngeal, and other anogenital cancers. The L1 protein, a major capsid protein of HPV, self-assembles into virus-like particles (VLPs) when expressed in heterologous systems such as yeast or insect cells. These VLPs mimic the native virus structure but lack viral DNA, rendering them non-infectious while retaining strong immunogenicity.
The use of recombinant DNA technology to produce L1 proteins revolutionized HPV vaccine development. Early studies demonstrated that L1-based VLPs elicit potent neutralizing antibodies by presenting conformational epitopes similar to those of the actual virus. This discovery led to the creation of prophylactic vaccines like Gardasil and Cervarix, which target high-risk HPV types (e.g., HPV-16. HPV-18) responsible for ~70% of cervical cancers. These vaccines have shown >90% efficacy in preventing HPV-related lesions.
Production of L1 recombinant proteins typically involves cloning the L1 gene into expression vectors, followed by purification and VLP assembly. Yeast (e.g., *Saccharomyces cerevisiae*) and baculovirus-insect cell systems are commonly used due to their scalability and post-translational modification capabilities. Advances in structural biology and genetic engineering have further optimized L1 stability and immunogenicity, enabling broader vaccine coverage against multiple HPV strains.
Beyond prevention, L1 recombinant proteins are explored in diagnostic tools and therapeutic vaccines. Their ability to induce robust immune responses also makes them candidates for combating other viral infections. Overall, L1-based technologies exemplify the success of recombinant protein platforms in addressing global health challenges, significantly reducing HPV-related morbidity and mortality worldwide.
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