| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SARM1 |
| Uniprot No | Q6SZW1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 559-702aa |
| 氨基酸序列 | GDTPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSVMGARNFVLVLSPGALDKCMQDHDCKDWVHKEIVTALSCGKNIVPIIDGFEWPEPQVLPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGR |
| 预测分子量 | 18.8 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3篇关于SARM1重组蛋白的关键文献概览：
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1. **文献名称**：*SARM1 is a metabolic sensor that triggers axonal degeneration through NAD+ depletion*
**作者**：Essuman, K. et al.
**摘要**：该研究首次揭示了SARM1蛋白的NADase(烟酰胺腺嘌呤二核苷酸酶)活性，证明其TIR结构域在激活后可催化NAD+水解，导致轴突内NAD+水平骤降，从而触发轴突变性。通过重组蛋白实验证实了SARM1的酶功能及其在神经退行性疾病中的关键作用。
2. **文献名称**：*Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules*
**作者**：Sasaki, Y. et al.
**摘要**：通过解析SARM1重组蛋白的晶体结构，揭示了其自抑制构象及激活机制。研究发现了SAM(sterile alpha motif)结构域与TIR结构域之间的相互作用如何维持SARM1的静息状态，并鉴定了可阻断其NADase活性的小分子抑制剂，为治疗神经损伤提供了潜在策略。
3. **文献名称**：*SARM1 autoactivation and enzymatic activity are directly regulated through its SAM domain*
**作者**：Gerdts, J. et al.
**摘要**：该研究利用重组SARM1蛋白阐明了其自激活机制，证明SAM结构域在调控SARM1活性中起关键作用。实验表明，SAM结构域的构象变化可解除自抑制，激活TIR结构域的NAD+水解功能，进而引发轴突退化，为干预SARM1相关疾病提供了理论依据。
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**备注**：上述文献均聚焦于SARM1的分子机制研究，涵盖其结构、酶活性及调控，对理解神经退行性疾病和开发靶向治疗具有重要意义。如需具体发表年份或期刊，可进一步补充关键词进行精准检索。
SARM1 (Sterile Alpha and TIR Motif-Containing Protein 1) is a NADase enzyme that plays a central role in axonal degeneration, a process linked to neurodegenerative disorders and nerve injury. Initially identified as a member of the MyD88-like TIR-domain protein family involved in innate immunity, SARM1 was later found to act as a key executioner of axonal self-destruction. Unlike other TLR adaptors, SARM1’s primary function in neurons revolves around its ability to deplete NAD+ (nicotinamide adenine dinucleotide), a critical metabolic cofactor, through its intrinsic enzymatic activity. Under normal conditions, SARM1 remains autoinhibited, but cellular stress signals (e.g., injury, metabolic imbalance) trigger its activation, initiating a local NAD+ depletion cascade that disrupts energy homeostasis and culminates in axonal fragmentation.
Recombinant SARM1 protein, typically produced in bacterial or insect cell expression systems, has become a vital tool for studying its structure, enzymatic mechanisms, and regulatory interactions. Researchers use purified SARM1 to characterize its TIR (Toll/interleukin-1 receptor) domain-driven NADase activity, map binding partners, and screen for inhibitors. Structural studies of recombinant SARM1 have revealed its multi-domain architecture, including ARM (Axon Degeneration Sterile Motif) and SAM (Sterile Alpha Motif) domains that regulate oligomerization and activation. Notably, the autoinhibitory mechanism and activation triggers (e.g., NMN accumulation, loss of NAD+) have been elucidated using recombinant systems. Such work informs therapeutic strategies targeting SARM1 to treat neurodegenerative diseases (e.g., ALS, glaucoma) or traumatic nerve injuries by blocking its NADase activity. Current challenges include understanding context-dependent regulatory switches and optimizing drug candidates that modulate SARM1 without disrupting its potential physiological roles in immunity or homeostasis.
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