| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NOD1 |
| Uniprot No | Q9Y239 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-953aa |
| 氨基酸序列 | MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICF |
| 预测分子量 | 107,6 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NOD1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan"*
**作者**：Girardin SE, et al.
**摘要**：该研究通过重组NOD1蛋白的体外实验，首次证实其特异性识别革兰氏阴性菌肽聚糖中的D-γ-谷氨酰基异二胺酸结构(iE-DAP)，揭示了NOD1作为先天免疫受体的分子识别机制。
2. **文献名称**：*"Reconstitution of the pathway for NF-κB activation by Nod1. a host protein mediating bacterial sensing"*
**作者**：Inohara N, et al.
**摘要**：利用重组NOD1蛋白在体外重建其信号通路，证明NOD1通过招募RIP2激酶激活NF-κB，并依赖CARD结构域的相互作用，为研究NOD1的免疫调控机制提供模型。
3. **文献名称**：*"Expression and purification of functional recombinant NOD1 leucine-rich repeat domain in Escherichia coli"*
**作者**：Bielig H, et al.
**摘要**：成功在大肠杆菌中表达并纯化重组NOD1的富亮氨酸重复结构域(LRR)，证实该结构域直接参与配体结合，为研究NOD1的配体识别提供结构基础。
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以上文献均围绕NOD1重组蛋白的功能、结构或信号机制展开，涵盖配体识别、通路重建及结构解析等方向。如需具体年份或期刊信息，可进一步补充检索。
NOD1 (Nucleotide-binding oligomerization domain-containing protein 1) is a cytosolic pattern recognition receptor (PRR) critical to the innate immune system. It belongs to the NOD-like receptor (NLR) family and functions as a sensor of bacterial peptidoglycan fragments, particularly γ-D-glutamyl-meso-diaminopimelic acid (iE-DAP), found in Gram-negative and certain Gram-positive bacteria. Structurally, NOD1 contains a C-terminal leucine-rich repeat (LRR) domain for ligand recognition, a central NACHT domain for oligomerization and ATPase activity, and an N-terminal caspase recruitment domain (CARD) for downstream signaling. Upon ligand binding, NOD1 self-oligomerizes and recruits RIPK2 (receptor-interacting serine/threonine-protein kinase 2), triggering activation of NF-κB and MAPK pathways to induce pro-inflammatory cytokine production.
Recombinant NOD1 proteins are engineered using expression systems (e.g., E. coli, HEK293 cells) to study its structural-functional relationships, ligand interactions, and signaling mechanisms. These proteins enable in vitro investigations into NOD1’s role in host-pathogen interactions, chronic inflammation, and autoimmune diseases. Research applications include screening for NOD1 agonists/antagonists, elucidating cross-talk with other immune receptors (e.g., TLRs), and exploring its involvement in conditions like inflammatory bowel disease or cancer. As a tool, recombinant NOD1 aids in deciphering its dual role in protective immunity and pathological inflammation, offering potential therapeutic targets for immune modulation. Studies also highlight its tissue-specific expression and polymorphisms linked to disease susceptibility.
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