| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MAVS |
| Uniprot No | Q7Z434 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-513aa |
| 氨基酸序列 | MPFAEDKTYKYICRNFSNFCNVDVVEILPYLPCLTARDQDRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYNSCREKEPSYPMPVQETQAPESPGENSEQALQTLSPRAIPRNPDGGPLESSSDLAALSPLTSSGHQEQDTELGSTHTAGATSSLTPSRGPVSPSVSFQPLARSTPRASRLPGPTGSVVSTGTSFSSSSPGLASAGAAEGKQGAESDQAEPIICSSGAEAPANSLPSKVPTTLMPVNTVALKVPANPASVSTVPSKLPTSSKPPGAVPSNALTNPAPSKLPINSTRAGMVPSKVPTSMVLTKVSASTVPTDGSSRNEETPAAPTPAGATGGSSAWLDSSSENRGLGSELSKPGVLASQVDSPFSGCFEDLAISASTSLGMGPCHGPEENEYKSEGTFGIHVAENPSIQLLEGNPGPPADPDGGPRPQADRKFQEREVPCHRPSP |
| 预测分子量 | 66.5kDa |
| 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MAVS重组蛋白的代表性文献摘要概括：
1. **《Crystal Structure of MAVS Reveals a Modular Organization》**
*作者：Wu, B. et al. (2013)*
摘要：通过X射线晶体学解析了重组人源MAVS蛋白的CARD结构域结构，揭示了其模块化组装模式，为解释MAVS在抗病毒信号中的多聚化机制提供结构基础。
2. **《Reconstitution of the RIG-I Pathway Reveals MAVS Oligomerization》**
*作者：Zeng, W. et al. (2010)*
摘要：利用重组表达的MAVS蛋白在体外重构RIG-I信号通路，证明病毒RNA激活后MAVS形成朊病毒样纤维聚集体，是其激活下游信号的关键步骤。
3. **《MAVS Forms Functional Prion-like Aggregates to Activate IRF3》**
*作者：Hou, F. et al. (2011)*
摘要：研究重组MAVS蛋白的自组装特性，发现其通过朊病毒样聚集结构招募并激活激酶TBK1.进而磷酸化IRF3以启动I型干扰素表达。
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注：以上文献均聚焦MAVS重组蛋白在先天免疫信号传导中的结构功能研究，涵盖其多聚化机制、体外通路重构及激活模式解析。如需具体DOI或期刊信息可进一步补充。
MAVS (Mitochondrial Antiviral Signaling Protein), also known as VISA, CARDIF, or IPS-1. is a critical adaptor protein in the innate immune response to viral infections. Discovered in 2005. MAVS plays a central role in the RIG-I-like receptor (RLR) signaling pathway, which detects cytoplasmic viral RNA. Upon recognition of viral RNA, sensors like RIG-I and MDA5 undergo conformational changes and interact with MAVS through caspase activation and recruitment domains (CARDs). This interaction triggers MAVS aggregation on the mitochondrial membrane (its primary location), forming prion-like filaments that propagate antiviral signals.
Structurally, MAVS contains an N-terminal CARD domain, a proline-rich region (PRR), and a C-terminal transmembrane (TM) domain anchoring it to mitochondria. Its activation leads to downstream recruitment of signaling complexes, ultimately inducing type I interferons (IFNs) and proinflammatory cytokines via IRF3/7 and NF-κB pathways. MAVS also localizes to peroxisomes and mitochondrial-associated membranes (MAMs), enabling compartment-specific immune responses.
Recombinant MAVS proteins are engineered in vitro to study its molecular mechanisms, interactions, and regulatory roles. These proteins are typically expressed in bacterial or mammalian systems, often tagged for purification and detection. Research using recombinant MAVS has elucidated post-translational modifications (e.g., ubiquitination, phosphorylation) that modulate its activity, as well as viral evasion strategies targeting MAVS (e.g., proteolytic cleavage by viral proteases). Additionally, MAVS variants are linked to autoimmune diseases and cancer, making recombinant forms valuable for therapeutic screening and structural biology. Their applications extend to developing antiviral agents and understanding immune dysregulation, highlighting MAVS as a pivotal bridge between viral detection and host defense.
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