| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NGAL |
| Uniprot No | P80188 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-198aa |
| 氨基酸序列 | QDSTSDLIPAPPLSKVPLQQNFQDNQFQGKWYVVGLAGNAILREDKDPQK MYATIYELKEDKSYNVTSVLFRKKKCDYWIRTFVPGCQPGEFTLGNIKSY PGLTSYLVRVVSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKE NFIRFSKSLGLPENHIVFPVPIDQCIDG |
| 预测分子量 | 21 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. |
1. **"Recombinant human neutrophil gelatinase-associated lipocalin (rhNGAL) for early detection of acute kidney injury"** - Author: Mori K, et al.
摘要：研究探讨重组人NGAL作为急性肾损伤早期生物标志物的潜力，验证其体外表达纯化方法及临床检测敏感性。
2. **"Expression and purification of functional recombinant NGAL in Escherichia coli"** - Author: Goetz DH, et al.
摘要：描述在大肠杆菌中高效表达可溶性NGAL重组蛋白的优化策略，验证其与铁载体结合的功能活性。
3. **"Lipocalin 2 regulates inflammation during pulmonary fibrosis through macrophage polarization"** - Author: Sunil VR, et al.
摘要：利用重组NGAL蛋白探究其在肺纤维化中的作用，发现其通过调控巨噬细胞极化影响炎症反应通路。
4. **"NGAL as a potential therapeutic target in breast cancer metastasis"** - Author: Yang J, et al.
摘要：通过体外实验证明重组NGAL蛋白可抑制乳腺癌细胞侵袭，机制涉及MMP-9信号通路调控。
Neutrophil gelatinase-associated lipocalin (NGAL), also known as lipocalin-2 or siderocalin, is a 25-kDa secretory protein belonging to the lipocalin family. It was initially identified in activated neutrophils and is involved in innate immunity, functioning as a bacteriostatic agent by sequestering iron-carrying siderophores, thereby limiting bacterial growth. NGAL is expressed in various tissues, including the kidney, liver, and epithelial cells, and its production is upregulated during pathological conditions such as inflammation, infection, and cancer.
Structurally, NGAL features a characteristic β-barrel fold that binds small hydrophobic molecules, including iron-bound siderophores. This iron-binding property links NGAL to cellular iron homeostasis and oxidative stress regulation. In clinical contexts, NGAL has gained attention as a sensitive biomarker for early detection of acute kidney injury (AKI), as its expression surges in renal tubules within hours of injury, preceding traditional markers like serum creatinine.
Recombinant NGAL is produced using expression systems such as *E. coli* or mammalian cell lines. Bacterial systems offer cost-effective yields but may lack post-translational modifications, while eukaryotic systems produce glycosylated forms closer to natural human NGAL. Purification typically involves affinity chromatography, ensuring high specificity and bioactivity.
Research applications of recombinant NGAL span disease modeling, therapeutic development, and diagnostic assays. It is studied for its dual roles in pathologies: protective effects in AKI by mitigating iron-mediated oxidative damage, and pro-tumorigenic effects in cancers by promoting cell survival, angiogenesis, and metastasis. Additionally, NGAL's ability to bind diverse molecules has inspired its engineering for drug delivery or targeted therapies.
Despite its promise, challenges remain in understanding context-dependent roles and optimizing clinical translation. Ongoing studies focus on elucidating signaling pathways, validating diagnostic thresholds, and exploring therapeutic modulation in renal diseases, cancer, and chronic inflammatory disorders.
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