| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MAK16 |
| Uniprot No | Q9BXY0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-300aa |
| 氨基酸序列 | MQSDDVIWDT LGNKQFCSFK IRTKTQSFCR NEYSLTGLCN RSSCPLANSQ YATIKEEKGQ CYLYMKVIER AAFPRRLWER VRLSKNYEKA LEQIDENLIY WPRFIRHKCK QRFTKITQYL IRIRKLTLKR QRKLVPLSKK VERREKRREE KALIAAQLDN AIEKELLERL KQDTYGDIYN FPIHAFDKAL EQQEAESDSS DTEEKDDDDD DEEDVGKREF VEDGEVDESD ISDFEDMDKL DASSDEDQDG KSSSEEEEEK ALSAKHKGKM PLRGPLQRKR AYVEIEYEQE TEPVAKAKTT |
| 预测分子量 | 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. |
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MAK16 is a conserved nucleocytoplasmic protein implicated in diverse cellular and viral processes, particularly RNA metabolism and virus-host interactions. Initially identified in Saccharomyces cerevisiae, it is recognized for its role in ribosome biogenesis and nucleocytoplasmic transport. Structurally, it contains a unique N-terminal domain with RNA-binding motifs and a C-terminal region critical for protein-protein interactions.
In virology, MAK16 gained attention as a host factor co-opted by certain RNA viruses, including members of the Orthomyxoviridae family (e.g., influenza viruses). Studies suggest it binds viral genomic RNA, facilitating replication complex assembly by bridging viral polymerase components and host machinery. Its interaction with viral nucleoproteins highlights its dual functionality in ribosomal RNA processing and viral replication.
Recombinant MAK16 proteins are typically produced using Escherichia coli or insect cell expression systems, enabling biochemical and structural studies. Purification often involves affinity chromatography followed by size-exclusion methods to isolate functional monomers. Crystallographic and cryo-EM analyses of recombinant MAK16 have revealed conformational flexibility, explaining its adaptability in binding heterogeneous RNA targets.
Current research leverages recombinant MAK16 to dissect virus-host interplay, screen antiviral compounds targeting MAK16-viral RNA interfaces, and explore its regulatory roles in cellular stress responses. Its conserved nature across eukaryotes makes it a model for studying evolutionary strategies of RNA-associated proteins. However, unresolved questions persist regarding its precise mechanistic contributions to ribosome maturation versus viral pathogenesis, driving ongoing investigations.
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