| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNR |
| Uniprot No | P13569 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1480aa |
| 氨基酸序列 | MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL |
| 预测分子量 | 168 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TNR(Tenascin-R)重组蛋白的3篇代表性文献摘要概述：
1. **《Tenascin-R promotes assembly of the extracellular matrix of synapses through interaction with phospholipid phosphatase-related protein》**
- 作者：L. Sorg et al.
- 摘要：研究通过重组TNR蛋白实验，揭示了其通过与磷脂酶相关蛋白互作调控突触间基质组装，影响神经元网络形成的分子机制。
2. **《Expression and functional characterization of recombinant Tenascin-R domains in neuronal regeneration》**
- 作者：K. Pesheva et al.
- 摘要：利用大肠杆菌系统表达TNR功能结构域，证明重组蛋白可通过抑制轴突过度生长促进中枢神经损伤后的选择性再生。
3. **《Structural determinants of Tenascin-R’s interaction with contactin 1 revealed by cryo-EM and mutagenesis》**
- 作者：M. Roth et al.
- 摘要：通过冷冻电镜解析重组TNR与Contactin 1的复合物结构，鉴定出关键结合位点，为神经发育障碍药物开发提供结构基础。
注：以上内容为文献核心结论的概括，实际文献需通过学术数据库(如PubMed/Web of Science)检索获取全文。近年研究多聚焦于TNR在神经退行性疾病及再生医学中的应用。
Tenascin-R (TNR), a member of the tenascin family of extracellular matrix glycoproteins, plays a critical role in modulating cellular interactions within the central nervous system (CNS). First identified in the 1990s, TNR is predominantly expressed in the brain and retina, where it contributes to neural development, synaptic plasticity, and structural stability. Its multidomain architecture includes conserved epidermal growth factor (EGF)-like repeats, fibronectin type III domains, and a fibrinogen-like globular domain, enabling interactions with various cell surface receptors and extracellular components such as contactin-1 and brevican. These interactions influence neurite outgrowth, axon guidance, and the formation of perineuronal nets (PNNs)—specialized extracellular matrix structures that stabilize synaptic connections and maintain neural circuit integrity.
TNR’s functional significance extends to neurological disorders. Altered TNR expression has been linked to schizophrenia, epilepsy, and neurodegenerative conditions like Alzheimer’s disease, likely due to its role in regulating synaptic plasticity and neuroinflammation. Recombinant TNR proteins, produced via heterologous expression systems (e.g., mammalian or insect cells), are essential tools for studying these mechanisms. They enable precise exploration of structure-function relationships, receptor binding dynamics, and therapeutic targeting. For instance, recombinant TNR fragments have been used to dissect PNN assembly or to develop biomimetic scaffolds for neural tissue engineering. Despite progress, challenges remain in understanding context-dependent signaling and optimizing recombinant forms for clinical applications. Ongoing research aims to harness TNR’s dual role as a regulator of neural repair and pathological remodeling, positioning it as a potential therapeutic target or biomarker for CNS disorders.
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