| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LGALS8 |
| Uniprot No | O00214 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-317aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMMLSLNNLQNIIYNPVIPFVGTIPDQLDPG TLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNT LINEKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRI GPEKIDTLGIYGKVNIHSIGFSFSSDLQSTQASSLELTEISRENVPKSGT PQLRLPFAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHL NPRLNIKAFVRNSFLQESWGEEERNITSFPFSPGMYFEMIIYCDVREFKV AVNGVHSLEYKHRFKELSSIDTLEINGDIHLLEVRSW |
| 预测分子量 | 38 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LGALS8(galectin-8)重组蛋白的3篇参考文献摘要：
1. **文献名称**：*Galectin-8 in TCR-mediated death of T cell hybridomas*
**作者**：Pardo E, et al.
**摘要**：该研究利用重组galectin-8蛋白，揭示了其在T细胞受体(TCR)信号通路中诱导T细胞杂交瘤凋亡的作用机制，表明其可能通过调控T细胞免疫稳态参与自身免疫疾病。
2. **文献名称**：*Recombinant human galectin-8 induces Jurkat T cell apoptosis by modulating caveolin-1/Akt signaling*
**作者**：Kim SJ, et al.
**摘要**：通过表达纯化的人源重组galectin-8蛋白，研究发现其能通过抑制caveolin-1/Akt通路激活caspase-3.从而诱导Jurkat T细胞凋亡，为癌症免疫治疗提供潜在靶点。
3. **文献名称**：*Structural and functional characterization of recombinant galectin-8 for antiviral drug discovery*
**作者**：Méndez-Huergo SP, et al.
**摘要**：该研究解析了重组galectin-8的晶体结构，并验证其通过结合病毒表面糖蛋白抑制多种包膜病毒(如HIV和HSV)进入宿主细胞的能力，为抗病毒药物开发奠定基础。
注：若需具体文献来源(期刊、年份等)，建议通过PubMed或Sci-Hub输入标题/作者进一步查询。
LGALS8. also known as galectin-8. is a member of the galectin family of β-galactoside-binding lectins that play diverse roles in cellular processes, including immune regulation, cell adhesion, and intracellular signaling. Encoded by the LGALS8 gene in humans, this tandem-repeat-type galectin contains two distinct carbohydrate-recognition domains (CRDs) connected by a linker peptide. It exists in both intracellular and secreted forms, interacting with glycoproteins and glycolipids to modulate biological functions.
Galectin-8 is notably involved in maintaining cellular homeostasis by acting as a danger sensor. It binds to exposed glycans on damaged lysosomes or vacuoles, triggering selective autophagy (lysophagy) to clear compromised organelles. Additionally, it participates in immune responses by regulating T-cell activity, neutrophil function, and pathogen recognition. Its role in cancer is dualistic, exhibiting both tumor-suppressive and pro-metastatic effects depending on context, often linked to interactions with cell surface receptors like integrins.
Recombinant LGALS8 protein is produced using expression systems (e.g., E. coli or mammalian cells) for functional studies. Researchers utilize it to investigate its binding specificity, signaling pathways (e.g., JNK, NF-κB), and therapeutic potential. It has shown promise in studies targeting infectious diseases, as it can interfere with viral entry (e.g., HIV, SARS-CoV-2) by binding viral envelopes or host receptors. In autoimmune diseases, galectin-8’s ability to modulate immune cell activity is being explored for drug development.
Current research focuses on its diagnostic applications, such as a biomarker for conditions like rheumatoid arthritis or cancer, and its therapeutic exploitation in immunotherapy or glycan-targeted treatments. The recombinant form enables precise mechanistic studies and high-throughput screening for inhibitors or enhancers of its activity, bridging structural biology and clinical translation.
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