| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MYPN |
| Uniprot No | Q86TC9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1320aa |
| 氨基酸序列 | MQDDSIEASTSISQLLRESYLAETRHRGNNERSRAEPSSNPCHFGSPSGAAEGGGGQDDLPDLSAFLSQEELDESVNLARLAINYDPLEKADETQARKRLSPDQMKHSPNLSFEPNFCQDNPRSPTSSKESPQEAKRPQYCSETQSKKVFLNKAADFIEELSSLFKSHSSKRIRPRACKNHKSKLESQNKVMQENSSSFSDLSERRERSSVPIPIPADTRDNEVNHALEQQEAKRREAEQAASEAAGGDTTPGSSPSSLYYEEPLGQPPRFTQKLRSREVPEGTRVQLDCIVVGIPPPQVRWYCEGKELENSPDIHIVQAGNLHSLTIAEAFEEDTGRYSCFASNIYGTDSTSAEIYIEGVSSSDSEGDPNKEEMNRIQKPNEVSSPPTTSAVIPPAVPQAQHLVAQPRVATIQQCQSPTNYLQGLDGKPIIAAPVFTKMLQNLSASEGQLVVFECRVKGAPSPKVEWYREGTLIEDSPDFRILQKKPRSMAEPEEICTLVIAEVFAEDSGCFTCTASNKYGTVSSIAQLHVRGNEDLSNNGSLHSANSTTNLAAIEPQPSPPHSEPPSVEQPPKPKLEGVLVNHNEPRSSSRIGLRVHFNLPEDDKGSEASSEAGVVTTRQTRPDSFQERFNGQATKTPEPSSPVKEPPPVLAKPKLDSTQLQQLHNQVLLEQHQLQNPPPSSPKEFPFSMTVLNSNAPPAVTTSSKQVKAPSSQTFSLARPKYFFPSTNTTAATVAPSSSPVFTLSSTPQTIQRTVSKESLLVSHPSVQTKSPGGLSIQNEPLPPGPTEPTPPPFTFSIPSGNQFQPRCVSPIPVSPTSRIQNPVAFLSSVLPSLPAIPPTNAMGLPRSAPSMPSQGLAKKNTKSPQPVNDDNIRETKNAVIRDLGKKITFSDVRPNQQEYKISSFEQRLMNEIEFRLERTPVDESDDEIQHDEIPTGKCIAPIFDKRLKHFRVTEGSPVTFTCKIVGIPVPKVYWFKDGKQISKRNEHCKMRREGDGTCSLHIESTTSDDDGNYTIMAANPQGRISCSGHLMVQSLPIRSRLTSAGQSHRGRSRVQERDKEPLQERFFRPHFLQAPGDMVAHEGRLCRLDCKVSGLPPPELTWLLNGQPVLPDASHKMLVRETGVHSLLIDPLTQRDAGTYKCIATNKTGQNSFSLELSVVAKEVKKAPVILEKLQNCGVPEGHPVRLECRVIGMPPPVFYWKKDNETIPCTRERISMHQDTTGYACLLIQPAKKSDAGWYTLSAKNEAGIVSCTARLDIYAQWHHQIPPPMSVRPSGSRYGSLTSKGLDIFSAFSSMESTMVYSCSSRSVVESDEL |
| 预测分子量 | 145,2 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MYPN重组蛋白的3篇代表性文献示例(注：以下内容为模拟虚构，实际文献需通过学术数据库查询)：
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1. **文献名称**: "Recombinant MYPN Protein Improves Cardiac Function in a Mouse Model of Dilated Cardiomyopathy"
**作者**: Tanaka K, et al.
**摘要**: 本研究通过大肠杆菌系统表达并纯化重组MYPN蛋白，验证其与肌联蛋白的结合能力。在扩张型心肌病模型小鼠中，注射重组MYPN可部分恢复心肌细胞收缩功能，提示其在治疗MYPN突变相关心肌病中的潜在应用。
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2. **文献名称**: "Structural and Functional Analysis of MYPN Mutants Using Recombinant Protein Expression"
**作者**: Chen L, et al.
**摘要**: 作者通过哺乳动物细胞系表达携带致病突变的重组MYPN蛋白，发现特定突变(如R100Q)导致蛋白稳定性下降及与肌动蛋白结合能力丧失，揭示了MYPN相关心肌病的分子机制。
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3. **文献名称**: "Development of a High-Yield Purification Protocol for Recombinant MYPN in Insect Cells"
**作者**: Müller S, et al.
**摘要**: 本文优化了杆状病毒-昆虫细胞系统中MYPN重组蛋白的表达与纯化工艺，获得高纯度蛋白用于晶体学研究。通过质谱和圆二色谱验证了蛋白正确折叠，为后续结构功能研究奠定基础。
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**备注**：实际文献需在PubMed、Google Scholar等平台以关键词“MYPN recombinant protein”或“MYPN expression”检索，并优先选择近5年发表的权威期刊研究。
**Background of MYPN Recombinant Protein**
MYPN (myopalladin) is a striated muscle-specific protein predominantly expressed in cardiac and skeletal muscles, where it plays a critical role in maintaining sarcomeric structure and function. As a component of the sarcomere, MYPN localizes to the Z-disc and I-band regions, interacting with key structural and signaling proteins such as α-actinin, nebulin, and calpain-3. These interactions are essential for sarcomere assembly, mechanical stability, and stress response mechanisms. MYPN also participates in transcriptional regulation by shuttling between the sarcomere and nucleus, influencing muscle-specific gene expression.
Mutations in the *MYPN* gene are linked to human cardiomyopathies, including dilated cardiomyopathy (DCM), hypertrophic cardiomyopathy (HCM), and restrictive cardiomyopathy (RCM), as well as skeletal myopathies. These pathogenic variants often disrupt protein-protein interactions or MYPN’s nuclear localization, leading to impaired sarcomere integrity, dysregulated signaling, and progressive muscle dysfunction.
Recombinant MYPN protein is generated using biotechnological platforms (e.g., bacterial, mammalian, or insect cell systems) to produce purified, functional protein for research and therapeutic exploration. Its applications include studying MYPN’s molecular interactions, elucidating disease mechanisms, and screening potential drugs targeting MYPN-related pathways. Additionally, recombinant MYPN serves as an antigen for antibody development or diagnostic assays.
Recent studies highlight MYPN’s emerging role in cardiac regeneration and its interaction with signaling pathways like TGF-β and MAPK, suggesting broader implications in muscle repair and remodeling. Ongoing research aims to leverage recombinant MYPN to advance precision therapies for genetic and acquired muscle disorders.
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