| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AFMID |
| Uniprot No | Q63HM1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-303aa |
| 氨基酸序列 | MMDVSGVGFP SKVPWKKMSA EELENQYCPS RWVVRLGAEE ALRTYSQIGI EATTRARATR KSLLHVPYGD GEGEKVDIYF PDESSEALPF FLFFHGGYWQ SGSKDESAFM VHPLTAQGVA VVIVAYGIAP KGTLDHMVDQ VTRSVAFVQK RYPSNKGIYL CGHSAGAHLA AMMLLADWTK HGVTPNLRGF FLVSGVFDLE PIVYTSQNVA LQLTLEDAQR NSPQLKVAQA QPVDPTCRVL VVVGQFDSPE FHRQSWEFYQ TLCQGEWKAS FEELHDVDHF EIVENLTQKD NVLTQIILKT IFQ |
| 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AFMID重组蛋白的3篇参考文献示例(内容为虚构，仅供格式参考)：
1. **文献名称**: *Expression and Characterization of Recombinant Human AFMID Protein in E. coli*
**作者**: Zhang L, et al.
**摘要**: 研究报道了通过大肠杆菌系统高效表达人源AFMID重组蛋白，并优化纯化条件获得高纯度蛋白。酶活实验证实其催化犬尿氨酸转化为邻氨基苯甲酸的活性，为后续功能研究奠定基础。
2. **文献名称**: *Structural Insights into AFMID’s Role in Tryptophan Metabolism*
**作者**: Johnson R, Patel S.
**摘要**: 通过X射线晶体学解析AFMID重组蛋白的三维结构，揭示了其底物结合域的关键氨基酸残基，结合分子动力学模拟阐明其在色氨酸代谢通路中的催化机制。
3. **文献名称**: *AFMID Recombinant Protein as a Potential Biomarker in Neurodegenerative Diseases*
**作者**: Lee H, et al.
**摘要**: 发现AFMID重组蛋白在帕金森病患者脑脊液中表达异常，体外实验表明其活性降低可能导致神经毒性代谢物积累，提示其作为疾病生物标志物的潜力。
(注：以上文献为示例，实际研究需查阅具体数据库。)
AFMID (arylformamidase) recombinant protein is a biotechnologically engineered enzyme derived from the AFMID gene, which encodes a hydrolase involved in the metabolism of arylformamide compounds. This protein plays a role in detoxification pathways by catalyzing the hydrolysis of formyl groups from aromatic amines, potentially mitigating the toxicity of environmental pollutants or endogenous metabolites. Its function is linked to the kynurenine pathway, indirectly influencing neurological processes through metabolite regulation.
Recombinant AFMID is typically produced using expression systems like *E. coli* or mammalian cells, enabling high-yield purification for research applications. The protein’s structure includes a conserved amidase domain, critical for substrate recognition and catalytic activity. Studies focus on its enzymatic kinetics, substrate specificity, and potential involvement in diseases such as cancer or neurodegenerative disorders, where altered kynurenine pathway metabolites are observed.
In drug discovery, AFMID recombinant protein serves as a tool to screen inhibitors or modulators targeting related metabolic pathways. It also aids in structural biology studies to resolve 3D configurations, guiding rational drug design. Despite its niche research scope, AFMID's role in bridging xenobiotic metabolism and disease mechanisms underscores its growing relevance in biomedical investigations.
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