| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LXN |
| Uniprot No | Q9BS40 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-222aa |
| 氨基酸序列 | MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYHLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFT FEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDY TILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE |
| 预测分子量 | 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LXN(Latexin)重组蛋白的3篇模拟参考文献示例(非真实文献，仅供格式参考)：
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1. **文献名称**: *"Recombinant LXN protein inhibits tumor growth by modulating inflammatory response in colorectal cancer"*
**作者**: Zhang Y, et al.
**摘要**: 本研究通过大肠杆菌表达系统成功纯化重组LXN蛋白，并发现其通过抑制NF-κB通路减少肿瘤微环境中炎症因子(如IL-6、TNF-α)的分泌，从而抑制结直肠癌细胞增殖及小鼠移植瘤生长。
2. **文献名称**: *"Structural and functional characterization of recombinant human Latexin in neuroprotection"*
**作者**: Lee S, et al.
**摘要**: 利用哺乳动物细胞体系表达人源LXN重组蛋白，解析其三维结构并验证其对神经元细胞的保护作用。实验表明，LXN通过结合金属羧肽酶M14家族成员，减少Aβ毒性诱导的神经元凋亡，提示其在阿尔茨海默病中的潜在应用。
3. **文献名称**: *"LXN重组蛋白对巨噬细胞极化的调控及其在自身免疫性疾病中的作用"*
**作者**: 王磊等.
**摘要**: 研究发现，重组LXN蛋白可促进巨噬细胞向M2型极化，降低促炎因子水平并上调IL-10表达，在类风湿性关节炎模型小鼠中显著缓解关节炎症，提示LXN或成为免疫调节治疗的新靶点。
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注：以上文献为模拟内容，实际研究中请通过PubMed、Web of Science等平台检索真实文献。
**Background of LXN (Latexin) Recombinant Protein**
LXN (latexin), a 25–30 kDa endogenous carboxypeptidase inhibitor, is encoded by the *LXN* gene in humans and conserved across vertebrates. Initially identified as an inhibitor of metallocarboxypeptidases like CPA4. it regulates peptide hormone processing and bioactive peptide degradation. Structurally, LXN contains a trefoil (TIL) domain, which mediates protein-protein interactions and stability, contributing to its multifunctional roles in inflammation, cancer, and tissue development.
Recombinant LXN protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) for functional studies. Its production enables exploration of LXN's physiological and pathological mechanisms. For example, LXN is downregulated in cancers (e.g., colorectal, breast) and acts as a tumor suppressor by modulating cell proliferation, apoptosis, and metastasis. In inflammatory contexts, LXN interacts with immune regulators, influencing macrophage polarization and cytokine secretion.
Research highlights LXN's involvement in stem cell differentiation, neuroprotection, and tissue regeneration. In neurodegenerative models, recombinant LXN demonstrates neuroprotective effects by inhibiting neuroinflammation and oxidative stress. Additionally, LXN regulates hematopoietic stem cell maintenance and adipocyte differentiation, suggesting roles in metabolic disorders.
Despite progress, LXN's signaling pathways remain partially defined. Its interaction with extracellular matrix components and receptors (e.g., integrins) hints at unexplored regulatory networks. Recombinant LXN serves as a critical tool for dissecting these pathways and developing therapeutic strategies. Notably, its dual role as a biomarker and therapeutic candidate is under investigation, particularly in cancer prognosis and regenerative medicine. Challenges include optimizing recombinant LXN stability and delivery for clinical applications. Overall, LXN recombinant protein bridges mechanistic insights and translational potential in biomedicine.
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