纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | KYNA |
Uniprot No | Q9HC97 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-309aa |
氨基酸序列 | MNGTYNTCGSSDLTWPPAIKLGFYAYLGVLLVLGLLLNSLALWVFCCRMQQWTETRIYMTNLAVADLCLLCTLPFVLHSLRDTSDTPLCQLSQGIYLTNRYMSISLVTAIAVDRYVAVRHPLRARGLRSPRQAAAVCAVLWVLVIGSLVARWLLGIQEGGFCFRSTRHNFNSMAFPLLGFYLPLAVVVFCSLKVVTALAQRPPTDVGQAEATRKAARMVWANLLVFVVCFLPLHVGLTVRLAVGWNACALLETIRRALYITSKLSDANCCLDAICYYYMAKEFQEASALAVAPSAKAHKSQDSLCVTLA |
预测分子量 | 34 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KYNA(犬尿喹啉酸)重组蛋白研究的3篇示例文献(内容为模拟概括,非真实文献):
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1. **文献名称**:*Recombinant kynurenine aminotransferase production in E. coli for enzymatic synthesis of neuroactive KYNA*
**作者**:Smith J, et al.
**摘要**:本研究利用大肠杆菌重组表达系统高效生产犬尿氨酸氨基转移酶(KAT),并优化其催化反应条件,实现了KYNA的规模化体外合成。实验表明重组KAT活性稳定,为神经科学研究提供了可靠的KYNA制备方法。
2. **文献名称**:*KYNA-mediated neuroprotection in ischemic stroke models using recombinant protein delivery*
**作者**:Chen L, et al.
**摘要**:通过重组蛋白递送技术将KYNA直接导入缺血性脑卒中小鼠模型,发现其显著抑制谷氨酸过度释放,减轻神经兴奋毒性,证实重组KYNA蛋白在神经保护中的潜在治疗价值。
3. **文献名称**:*Engineering a bifunctional recombinant enzyme for simultaneous kynurenine pathway modulation and KYNA synthesis*
**作者**:Garcia R, et al.
**摘要**:设计并表达了一种双功能重组融合蛋白,整合犬尿氨酸羟化酶与KAT活性,可在单一步骤中调控犬尿氨酸代谢通路并定向生成KYNA,为代谢性疾病研究提供新工具。
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**说明**:以上文献为示例性概括,实际研究中建议通过PubMed、Web of Science等平台以关键词"recombinant kynurenic acid protein"或"kynurenine aminotransferase expression"检索最新文献。
**Background of KYNA Recombinant Protein**
Kynurenic acid (KYNA), a metabolite of the tryptophan degradation pathway via the kynurenine pathway, is an endogenous neuroactive compound with multifaceted roles in physiological and pathological processes. It functions as a competitive antagonist of excitatory neurotransmitter receptors, including the N-methyl-D-aspartate (NMDA) receptor and the α7 nicotinic acetylcholine receptor, and modulates glutamatergic and cholinergic signaling. KYNA's involvement in neuroprotection, immune regulation, and redox balance has linked it to neurological disorders (e.g., schizophrenia, Alzheimer’s disease) and inflammatory conditions.
Recombinant KYNA-related proteins, such as enzymes in its biosynthesis (e.g., kynurenine aminotransferases, KATs) or proteins interacting with KYNA, are engineered using biotechnological platforms (e.g., *E. coli*, mammalian cell systems) to study its mechanistic pathways or therapeutic potential. These recombinant proteins enable high-purity, scalable production for structural analysis, drug screening, and functional assays. For instance, recombinant KAT isoforms help elucidate tissue-specific KYNA production, while engineered proteins mimicking KYNA’s receptor interactions aid in developing neuroprotective agents.
Current research focuses on leveraging KYNA recombinant proteins to explore therapeutic strategies targeting neuroinflammation, cognitive deficits, and neurodegenerative diseases. Challenges include optimizing protein stability and mimicking endogenous post-translational modifications. Advances in protein engineering and CRISPR-based models may further enhance their application in precision medicine and biomarker discovery.
In summary, KYNA recombinant proteins serve as critical tools for decoding KYNA's complex biology and translating its regulatory functions into clinical interventions.
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