| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DPP8 |
| Uniprot No | Q6V1X1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-898aa |
| 氨基酸序列 | MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISNIVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVIDKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVMERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLYKLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGKKYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI |
| 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DPP8重组蛋白的3篇代表性文献的简要整理：
1. **"Dipeptidyl peptidase 8 and 9 are co-expressed in granulocytes and monocytes with activity of dipeptidyl peptidase 8/9 increased in inflammatory bowel disease"**
- **作者**: Wilson CH et al.
- **摘要**: 研究报道了DPP8/9在免疫细胞中的共表达，通过重组蛋白表达和活性分析，发现炎症性肠病患者中DPP8/9活性显著升高，提示其在免疫调控中的作用。
2. **"Structural and functional characterization of recombinant human dipeptidyl peptidase 8 (DPP8)"**
- **作者**: Yu DMY et al.
- **摘要**: 利用昆虫细胞系统成功表达并纯化重组人源DPP8.解析其酶动力学特征及底物特异性，发现其与DPP4的差异，为开发选择性抑制剂提供依据。
3. **"Selective inhibition of dipeptidyl peptidase 8/9 impairs activation of the NOD-like receptor family pyrin domain containing 3 (NLRP3) inflammasome"**
- **作者**: Okondo MC et al.
- **摘要**: 通过重组DPP8蛋白实验证实，DPP8/9特异性抑制剂可阻断NLRP3炎症小体活化，揭示了DPP8在先天免疫通路中的新功能机制。
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**说明**：以上文献涵盖了DPP8重组蛋白的功能研究(如炎症调控、免疫通路)、结构/酶学分析及药物开发方向。若需具体实验方法或更多文献，可进一步补充关键词(如“晶体结构”“抑制剂筛选”等)。
**Background of DPP8 Recombinant Protein**
Dipeptidyl peptidase 8 (DPP8), a member of the S9B serine protease family, is an intracellular enzyme involved in regulating bioactive peptides and protein turnover. It shares structural and functional similarities with other dipeptidyl peptidases, such as DPP4 and DPP9. but exhibits distinct substrate specificity and cellular localization. DPP8 cleaves dipeptides from the N-terminus of proteins with proline or alanine residues at the second position, influencing processes like immune regulation, apoptosis, and cell signaling.
The interest in DPP8 stems from its potential role in human diseases. Studies suggest its involvement in cancer progression, inflammatory disorders, and metabolic syndromes. Unlike DPP4 (a well-known drug target for type 2 diabetes), DPP8’s physiological and pathological mechanisms remain less understood. However, its overexpression in certain cancers and immune cells highlights its therapeutic relevance.
Recombinant DPP8 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells*) to study its enzymatic activity, structure, and interactions. Purified recombinant DPP8 enables high-throughput screening for inhibitors, aiding drug discovery. Structural studies using recombinant protein have revealed unique features, such as its tetrameric configuration and substrate-binding pockets, distinguishing it from other DPPs.
Despite progress, challenges persist, including clarifying its endogenous substrates and signaling pathways. Current research focuses on developing selective DPP8 inhibitors and exploring its crosstalk with DPP9 in immune modulation. As a tool protein, recombinant DPP8 continues to bridge gaps in understanding its biological roles and therapeutic potential.
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