| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | QPCT |
| Uniprot No | Q16769 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-361aa |
| 氨基酸序列 | VSPSASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLHL |
| 预测分子量 | 41.8 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QPCT重组蛋白的3篇参考文献，涵盖结构、功能及应用研究：
1. **Schilling, S. et al. (2008)**
*Glutaminyl Cyclase Knockout Mice Exhibit Hypothalamic Neuroendocrine Deficits*
研究通过重组QPCT蛋白分析其催化机制，发现该酶在神经肽修饰中起关键作用，并构建基因敲除模型揭示其与内分泌功能紊乱的关联。
2. **Höfling, C. et al. (2016)**
*Crystal Structure of Human Glutaminyl Cyclase in Complex with a Substrate-derived Inhibitor*
利用重组QPCT蛋白进行X射线晶体学研究，解析其三维结构并阐明底物结合位点，为开发阿尔茨海默病靶向抑制剂提供结构基础。
3. **Cynis, H. et al. (2011)***
*Inhibition of Glutaminyl Cyclase Reduces pyroGlutamate Aβ in Alzheimer’s Disease Models*
通过重组QPCT蛋白验证其在淀粉样蛋白异常修饰中的作用，证明其抑制剂可减少病理蛋白沉积，提示潜在治疗价值。
注：文献年份及作者团队为示例性归纳，实际引用时建议通过PubMed或Web of Science核对最新研究。
**Background on QPCT Recombinant Protein**
QPCT (glutaminyl-peptide cyclotransferase) is an enzyme that catalyzes the formation of pyroglutamate (pGlu) residues at the N-terminus of specific peptides and proteins. This post-translational modification enhances the stability and biological activity of substrates, including hormones, neuropeptides, and chemokines. For instance, QPCT-mediated pyroglutamylation is critical for the function of chemokines like CXCL12 and CCL2. which play roles in immune responses, cancer metastasis, and inflammatory diseases. Dysregulation of QPCT has been linked to pathological conditions such as Alzheimer’s disease, where pGlu-modified amyloid-β peptides exhibit increased aggregation and neurotoxicity.
Recombinant QPCT proteins are engineered using biotechnological platforms (e.g., E. coli or mammalian expression systems) to produce highly pure, functional enzymes for research and therapeutic applications. These proteins retain the catalytic activity of native QPCT, enabling studies on enzyme kinetics, substrate specificity, and inhibitor screening. The development of QPCT recombinant tools has accelerated drug discovery efforts, particularly in targeting neurodegenerative diseases and inflammation. Inhibitors of QPCT, designed using recombinant enzyme assays, show potential in reducing harmful pGlu-amyloid-β levels in Alzheimer’s models.
Additionally, recombinant QPCT is utilized in structural biology to elucidate its mechanism, including its dependence on metal ions (e.g., zinc) for activity. Understanding QPCT’s molecular interactions aids in designing modulators to intervene in disease pathways. As a versatile biotechnological reagent, recombinant QPCT bridges basic research and clinical translation, offering insights into both physiological processes and therapeutic strategies for QPCT-associated disorders.
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