纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | NIPSNAP1 |
Uniprot No | Q9BPW8 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-284aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAPRLCSISVTARRLLGGPGPRAGDVA SAAAARFYSKDNEGSWFRSLFVHKVDPRKDAHSTLLSKKETSNLYKIQFH NVKPEYLDAYNSLTEAVLPKLHLDEDYPCSLVGNWNTWYGEQDQAVHLWR FSGGYPALMDCMNKLKNNKEYLEFRRERSQMLLSRRNQLLLEFSFWNEPQ PRMGPNIYELRTYKLKPGTMIEWGNNWARAIKYRQENQEAVGGFFSQIGE LYVVHHLWAYKDLQSREETRNAAWRKRGWDENVYYTVPLVRHMESRIMIP LKISPLQ |
预测分子量 | 36 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NIPSNAP1重组蛋白的3篇参考文献及其摘要概述:
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1. **文献名称**:*Structural and functional analysis of the NIPSNAP1 protein implicated in mitochondrial dynamics*
**作者**:Smith A, et al.
**摘要**:通过重组表达纯化人源NIPSNAP1蛋白,解析其晶体结构,揭示其与线粒体膜蛋白相互作用的关键结构域,并证明其在调控线粒体分裂中的功能。
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2. **文献名称**:*NIPSNAP1 regulates autophagosome-lysosome fusion through interaction with ATG8 family proteins*
**作者**:Chen L, et al.
**摘要**:研究利用重组NIPSNAP1蛋白进行体外结合实验,发现其通过LC3相互作用基序(LIR)与自噬相关蛋白ATG8结合,促进自噬小体与溶酶体的融合过程。
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3. **文献名称**:*NIPSNAP1 as a redox sensor: Role in Parkinson’s disease pathogenesis*
**作者**:Kimura T, et al.
**摘要**:通过重组NIPSNAP1蛋白的氧化还原特性研究,发现其在帕金森病模型中响应氧化应激,调控多巴胺能神经元的存活,提示其作为治疗靶点的潜力。
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注:以上文献为示例,实际引用时建议通过PubMed或Web of Science检索最新研究。
**Background of NIPSNAP1 Recombinant Protein**
NIPSNAP1 (NipSnap homolog 1) is a conserved protein belonging to the NIPSNAP family, characterized by a unique structural fold resembling the tetratricopeptide repeat (TPR) domain. It is ubiquitously expressed across tissues, with notable roles in cellular processes such as vesicular trafficking, mitochondrial dynamics, and autophagy. Structurally, NIPSNAP1 contains a N-terminal β-propeller domain and a C-terminal α-helical region, facilitating interactions with diverse molecular partners, including proteins involved in membrane trafficking (e.g., RAB GTPases) and autophagy (e.g., ATG8/LC3 family proteins).
Functionally, NIPSNAP1 has been implicated in mitochondrial quality control. It localizes to mitochondria and participates in mitophagy by recruiting autophagy machinery during stress, acting as a "eat-me" signal for damaged mitochondria. Additionally, it regulates lysosomal function and endosomal sorting, linking it to neurodegenerative diseases like Parkinson’s, where disrupted protein clearance mechanisms are critical.
Recombinant NIPSNAP1 protein is engineered for *in vitro* studies to dissect its molecular interactions, structural features, and functional roles. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), it retains post-translational modifications crucial for activity when expressed in eukaryotic hosts. This recombinant tool enables investigations into its binding partners, enzymatic assays, and screening for small-molecule modulators.
Emerging evidence highlights NIPSNAP1’s dual role in cancer—acting as a tumor suppressor in certain contexts (e.g., colorectal cancer) while promoting progression in others (e.g., glioblastoma). Its recombinant form aids in elucidating these context-dependent mechanisms and exploring therapeutic targeting. Overall, NIPSNAP1 recombinant protein serves as a vital resource for unraveling its multifaceted roles in health and disease.
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