| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LYG2 |
| Uniprot No | Q86SG7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-212aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSSYPFSHS MKPHLHPRLY HGCYGDIMTM KTSGATCDAN SVMNCGIRGS EMFAEMDLRA IKPYQTLIKE VGQRHCVDPA VIAAIISRES HGGSVLQDGW DHRGLKFGLM QLDKQTYHPV GAWDSKEHLS QATGILTERI KAIQKKFPTW SVAQHLKGGL SAFKSGIEAI ATPSDIDNDF VNDIIARAKF YKRQSF |
| 预测分子量 | 24 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. |
以下是几篇关于LYG2重组蛋白的模拟参考文献示例(注：LYG2相关研究目前公开数据有限，以下内容为模拟构造，建议通过PubMed、Google Scholar等平台查阅真实文献)：
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1. **文献名称**: "Recombinant LYG2 protein inhibits tumor growth by modulating immune response in colorectal cancer"
**作者**: Chen X, Wang Y, et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化了LYG2重组蛋白，证实其通过激活CD8+ T细胞和抑制调节性T细胞(Tregs)增强抗肿瘤免疫反应，在结肠癌小鼠模型中显著抑制肿瘤生长。
2. **文献名称**: "LYG2 as a novel biomarker: Expression profiling and functional analysis in lung adenocarcinoma"
**作者**: Liu H, Zhang R, et al.
**摘要**: 通过免疫组化和Western blot分析，发现LYG2在肺腺癌组织中低表达，且与患者预后正相关。重组LYG2蛋白在体外实验中被证明可诱导癌细胞凋亡并抑制迁移。
3. **文献名称**: "Structural characterization and antibacterial activity of recombinant LYG2 protein from oyster hemolymph"
**作者**: Li M, Sun J, et al.
**摘要**: 首次从牡蛎血淋巴中克隆LYG2基因，并在真核表达系统中获得重组蛋白。该蛋白表现出广谱抗菌活性，尤其对革兰氏阴性菌(如大肠杆菌)具有显著抑制作用。
4. **文献名称**: "LYG2 interacts with PD-L1 and disrupts immune checkpoint signaling in melanoma"
**作者**: Kim S, Park JH, et al.
**摘要**: 研究发现重组LYG2蛋白可通过结合PD-L1阻断其与PD-1的相互作用，逆转肿瘤微环境中的T细胞耗竭，为黑色素瘤的免疫治疗提供了新策略。
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**建议**：若需真实文献，可访问以下数据库检索关键词：
- 搜索词：`"LYG2" AND "recombinant protein"`
- 数据库：PubMed (https://pubmed.ncbi.nlm.nih.gov) / ScienceDirect (https://www.sciencedirect.com)
LYG2 (Lysozyme G-like 2), a member of the lysozyme superfamily, is a secreted protein encoded by the *LYG2* gene in humans. Lysozymes are evolutionarily conserved enzymes known for their antimicrobial properties, particularly in breaking down bacterial cell walls by hydrolyzing β-1.4-glycosidic bonds in peptidoglycan. While the canonical lysozyme (e.g., LYZ) is well-characterized, LYG2 represents a less-studied isoform with distinct structural and functional features. Its recombinant form is engineered to enable large-scale production and functional studies.
Recombinant LYG2 protein is typically produced using heterologous expression systems, such as *E. coli* or mammalian cell cultures, followed by purification via affinity chromatography. Structural analyses suggest that LYG2 retains a conserved glycohydrolase domain but may exhibit unique substrate preferences or binding motifs compared to other lysozymes. Emerging evidence highlights its potential role in innate immunity, particularly in mucosal surfaces, where it may act synergistically with other antimicrobial peptides. Additionally, LYG2 has been implicated in cancer biology, with studies showing altered expression in certain tumors, though its mechanistic contributions remain unclear.
Research on recombinant LYG2 focuses on deciphering its biological functions, including antibacterial activity, immunomodulatory effects, and possible involvement in disease pathways. Its recombinant form serves as a critical tool for *in vitro* assays, antibody development, and preclinical models. Challenges in production, such as protein solubility and post-translational modifications, are often addressed through codon optimization or engineered cell lines. As interest in host-defense proteins grows, LYG2 recombinant protein holds promise for therapeutic applications, such as combating antibiotic-resistant infections or modulating immune responses in chronic inflammatory conditions. Further studies are needed to fully elucidate its physiological roles and translational potential.
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