| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NAPSA |
| Uniprot No | O96009 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 64-420aa |
| 氨基酸序列 | KPIFVPLSNYRDVQYFGEIGLGTPPQNFTVAFDTGSSNLWVPSRRCHFFSVPCWLHHRFDPKASSSFQANGTKFAIQYGTGRVDGILSEDKLTIGGIKGASVIFGEALWEPSLVFAFAHFDGILGLGFPILSVEGVRPPMDVLVEQGLLDKPVFSFYLNRDPEEPDGGELVLGGSDPAHYIPPLTFVPVTVPAYWQIHMERVKVGPGLTLCAKGCAAILDTGTSLITGPTEEIRALHAAIGGIPLLAGEYIILCSEIPKLPAVSFLLGGVWFNLTAHDYVIQTTRNGVRLCLSGFQALDVPPPAGPFWILGDVFLGTYVAVFDRGDMKSSARVGLARARTRGADLGWGETAQAQFPG |
| 预测分子量 | 42.5kDa |
| 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NAPSA(Napsin A aspartic peptidase)重组蛋白的模拟参考文献示例(仅供参考，建议通过学术数据库核实具体文献)：
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1. **标题**: *"Expression and Purification of Recombinant Napsin A for Functional Studies"*
**作者**: Smith J, et al.
**摘要**: 本研究描述了在大肠杆菌中高效表达和纯化重组人Napsin A蛋白的方法，验证了其酶活性及在肺腺癌生物标志物研究中的应用潜力。
2. **标题**: *"Structural Characterization of Recombinant NAPSA and Its Role in Proprotein Processing"*
**作者**: Lee H, et al.
**摘要**: 通过X射线晶体学解析了重组NAPSA的三维结构，探讨其在天冬氨酸蛋白酶家族中的独特催化机制及其在前体蛋白成熟中的作用。
3. **标题**: *"Development of a NAPSA-Specific Monoclonal Antibody Using Recombinant Protein Antigen"*
**作者**: Zhang Y, et al.
**摘要**: 利用重组NAPSA蛋白作为抗原，成功制备高特异性单克隆抗体，并验证其在免疫组化中对肺组织病理诊断的准确性。
4. **标题**: *"Recombinant Napsin A as a Therapeutic Target in Renal Cell Carcinoma"*
**作者**: Gupta R, et al.
**摘要**: 研究重组NAPSA在肾癌细胞中的异常表达，揭示其作为潜在治疗靶点的功能，并通过体外实验验证抑制剂对其酶活性的调控作用。
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**注意**：以上文献为示例性质，实际研究需通过PubMed、Web of Science等平台以关键词“recombinant NAPSA”或“napsin A recombinant”检索最新成果。如需具体文献，可提供更详细的研究方向以便进一步筛选。
Napsin A Aspartic Peptidase (NAPSA), also known as kidney-derived aspartic protease or KAP, is a protease enzyme belonging to the aspartic peptidase family. It is encoded by the *NAPSA* gene in humans and is primarily expressed in the lung, kidney, and thyroid tissues. Structurally, NAPSA is synthesized as a zymogen (proenzyme) that undergoes proteolytic cleavage to become active. Its catalytic activity relies on two conserved aspartic acid residues within its active site, characteristic of aspartic proteases.
Functionally, NAPSA plays a critical role in the maturation of pulmonary surfactant protein B (SP-B), a lipid-protein complex essential for reducing alveolar surface tension and maintaining respiratory function. In the kidney, it is implicated in protein degradation and cellular homeostasis. Notably, NAPSA has garnered attention in biomedical research due to its tissue-specific expression patterns and potential clinical relevance. It is frequently studied as a biomarker for lung adenocarcinoma, as its expression is significantly downregulated in many pulmonary malignancies, aiding in differential diagnosis and prognosis assessment.
Recombinant NAPSA protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to ensure high purity and bioactivity. This engineered protein retains the enzymatic properties of native NAPSA, enabling its use in functional studies, inhibitor screening, and antibody development. Researchers employ recombinant NAPSA to explore its physiological roles, interactions with substrates, and regulatory mechanisms in diseases like cancer or pulmonary disorders. Additionally, it serves as a critical reagent in diagnostic assays to detect NAPSA-specific antibodies or quantify its expression levels in clinical samples.
The development of recombinant NAPSA has advanced both basic and translational research, offering insights into its dual roles in normal physiology and pathology. Its applications extend to therapeutic target validation and biomarker discovery, underscoring its importance in respiratory and oncology research.
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