| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | SNX13 |
| Uniprot No | Q6PHS6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-957aa |
| 氨基酸序列 | MLTEASLSIWGWGSLGIVLFLITFGPFVIFYLAFYILCFVGGGLVVTLLYGKTNSEKYLEQCEHSFLPPTSSGVPKCLEEMKREARTIKIDRRLTGANIIDEPLQQVIQFSLRDYVQYWYYTLSDDESFLLEIRQTLQNALIQFATRSKEIDWQPYFTTRIVDDFGTHLRVFRKAQQRVTEKDDQVKGTAEDLVETFFEVEVEMEKDVCRDLVCTSPKDEEGFLRDLCEVLLYLLLPPGDFQSKIMRYFVREILARGILLPLINQLSDPDYINQYVIWMIRDSNCNYEAFMNIIKLSDNIGELEAVRDKAAEELQYLRSLDTAGDDINTIKNQINSLLFVKKVCDSRIQRLQSGKEINTVKLAANFGKLCTVPLDSILVDNVALQFFMDYMQQTGGQAHLFFWMTVEGYRVTAQQQLEVLSGRQRDGKQQTNQTKGLLRAAAVGIYEQYLSEKASPRVTVDDYLVAKLADTLNHEDPTPEIFDDIQRKVYELMLRDERFYPSFRQNALYVRMLAELDMLKDPSFRGSDDGDGESFNGSPTGSINLSLDDLSSVTSDDSVQLHAYISDTGVCNDHGKTYALYAITVHRRNLNTEEMWKTYRRYSDFHDFHMRITEQFENLSSILKLPGKKTFNNMDRDFLEKRKKDLNAYLQLLLTPEMMKASPALAHCVYDFLENKAYSKGKGDFARKMDTFVNPLRNSMRNVSNAVKSLPDSLAEGVTKMSDNVGRMSERLGQDIKQSFFKVPPLITKTDSDPEHCRVSAQLDDNVDDNIPLRVMLLLMDEVFDLKERNQWLRRNIKNLLQQLIRATYGDTINRKIVDHVDWMTSPEQVADSVKRFRDAFWPNGILAETVPCRDKAIRMRTRIAGKTKLFAIMPDELKHIIGAETTRKGILRVFEMFQHNQLNRRMVYVFLEGFLETLFPQYKFRELFNKLHSRSKQMQKYKQKLQSTQAPSLQKR |
| 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. |
以下是关于SNX13重组蛋白的3篇参考文献示例(内容为虚构模拟，仅作格式参考)：
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1. **文献名称**: *SNX13 regulates endosomal trafficking through its phosphoinositide-binding domain*
**作者**: Li X, Wang Y, Chen Z
**摘要**: 本研究解析了SNX13重组蛋白的PX结构域与磷脂酰肌醇的结合机制，发现其通过识别特定膜脂成分调控内体分选过程，并利用重组蛋白验证了其在内体膜形态形成中的作用。
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2. **文献名称**: *Structural and functional characterization of recombinant SNX13 in autophagy*
**作者**: Kumar S, et al.
**摘要**: 通过体外表达SNX13重组蛋白，结合冷冻电镜技术揭示了其与自噬相关蛋白LC3的相互作用界面，证明SNX13在自噬体成熟中具有调控功能。
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3. **文献名称**: *SNX13 deficiency disrupts cholesterol homeostasis: Insights from recombinant protein assays*
**作者**: Garcia R, et al.
**摘要**: 利用重组SNX13蛋白进行脂质结合实验，发现其BAR结构域参与胆固醇转运，并证明SNX13缺失会导致细胞胆固醇代谢异常，与动脉粥样硬化发病相关。
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注：以上文献信息为示例性虚构内容，实际研究中请通过PubMed、Google Scholar等平台检索真实文献。
SNX13 (Sorting Nexin 13) is a member of the sorting nexin family, a group of proteins involved in membrane trafficking, endosomal sorting, and cellular signaling. These proteins typically contain a conserved phox homology (PX) domain that binds to phosphoinositides, enabling their recruitment to specific membrane compartments. SNX13 is distinguished by its unique structural features, including an N-terminal PX domain, a central region with a putative BAR (Bin/Amphiphysin/Rvs) domain, and a C-terminal domain with potential regulatory functions. It plays a critical role in retrograde transport from endosomes to the trans-Golgi network (TGN), lipid metabolism, and autophagy regulation.
Recombinant SNX13 protein is engineered for in vitro studies to dissect its molecular interactions, structural dynamics, and functional mechanisms. Its production typically involves heterologous expression systems (e.g., E. coli, mammalian cells) followed by purification to homogeneity. Researchers utilize recombinant SNX13 to investigate its binding partners, such as retromer complex components, and its role in trafficking cargo proteins like cation-independent mannose-6-phosphate receptor (CI-M6PR). Dysregulation of SNX13 has been linked to diseases, including Niemann-Pick type C (NPC), a lysosomal storage disorder, where impaired cholesterol trafficking is associated with pathogenic mutations in SNX13-interacting proteins.
Studies also highlight SNX13’s involvement in cellular stress responses and cancer progression, where altered expression correlates with tumorigenesis. Recombinant SNX13 serves as a tool for drug discovery, enabling high-throughput screening for compounds targeting endosomal pathways. Structural analysis of the recombinant protein has provided insights into its lipid-binding specificity and conformational changes during membrane remodeling. Overall, SNX13 recombinant protein is pivotal for advancing our understanding of intracellular trafficking networks and their implications in health and disease.
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