| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLC35F3 |
| Uniprot No | Q8IY50 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-421aa |
| 氨基酸序列 | MKKHSARVAPLSACNSPVLTLTKVEGEERPRDSPGPAEAQAPAGVEAGGRASRRCWTCSRAQLKKIFWGVAVVLCVCSSWAGSTQLAKLTFRKFDAPFTLTWFATNWNFLFFPLYYVGHVCKSTEKQSVKQRYRECCRFFGDNGLTLKVFFTKAAPFGVLWTLTNYLYLHAIKKINTTDVSVLFCCNKAFVFLLSWIVLRDRFMGVRIVAAILAIAGIVMMTYADGFHSHSVIGIALVVASASMSALYKVLFKLLLGSAKFGEAALFLSILGVFNILFITCIPIILYFTKVEYWSSFDDIPWGNLCGFSVLLLTFNIVLNFGIAVTYPTLMSLGIVLSIPVNAVIDHYTSQIVFNGVRVIAIIIIGLGFLLLLLPEEWDVWLIKLLTRLKVRKKEEPAEGAADLSSGPQSKNRRARPSFAR |
| 预测分子量 | 46.8kDa |
| 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SLC35F3重组蛋白的参考文献示例(因实际文献有限，部分内容为模拟结构，建议通过学术数据库进一步检索)：
1. **文献名称**：*Functional characterization of SLC35F3 as a lysosomal thiamine transporter*
**作者**：K. Tanaka et al.
**摘要**：研究通过重组蛋白表达技术，解析了SLC35F3在溶酶体膜上的定位及其硫胺素(维生素B1)转运功能，揭示了其在细胞能量代谢中的潜在作用。
2. **文献名称**：*SLC35F3 overexpression promotes cancer cell proliferation via enhanced iron uptake*
**作者**：L. Zhang et al.
**摘要**：该文献报道了重组SLC35F3蛋白在肿瘤细胞中的异常表达，并证明其通过调控铁离子转运促进肿瘤细胞增殖，为癌症治疗提供了新靶点。
3. **文献名称**：*Structural insights into SLC35F3 substrate specificity by cryo-EM*
**作者**：M. Chen et al.
**摘要**：利用冷冻电镜技术解析了重组SLC35F3蛋白的三维结构，阐明了其底物结合域的关键氨基酸残基及转运机制。
4. **文献名称**：*SLC35F3 variants link to neurodegenerative disorders via impaired lysosomal function*
**作者**：R. Gupta et al.
**摘要**：通过重组蛋白功能实验，发现SLC35F3基因突变导致溶酶体运输障碍，可能与帕金森病等神经退行性疾病相关。
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**注意**：以上为模拟示例，实际文献需通过PubMed/Google Scholar等平台以“SLC35F3 recombinant protein”或相关关键词检索。建议优先选择近5年发表的研究以获取最新进展。
**Background of SLC35F3 Recombinant Protein**
SLC35F3 (Solute Carrier Family 35 Member F3) belongs to the SLC35 family of nucleotide sugar transporters (NSTs), which facilitate the translocation of nucleotide sugars from the cytoplasm into the lumen of the Golgi apparatus and endoplasmic reticulum. These transporters are critical for glycosylation, a post-translational modification essential for protein folding, cellular communication, and membrane integrity. SLC35F3. though less characterized than other family members, is hypothesized to transport specific nucleotide sugars, such as UDP-galactose or UDP-N-acetylglucosamine, contributing to glycoprotein and glycolipid biosynthesis.
The gene encoding SLC35F3 is located on human chromosome 1 and is expressed in various tissues, including the liver, brain, and kidneys. Dysregulation of SLC transporters is often linked to metabolic disorders, cancer, and neurodegenerative diseases. While SLC35F3's exact physiological role remains under investigation, preliminary studies suggest its involvement in cellular homeostasis and stress responses. For instance, altered SLC35F3 expression has been observed in certain cancers, hinting at potential roles in tumor progression or drug resistance.
Recombinant SLC35F3 protein is engineered for in vitro studies to elucidate its structure, substrate specificity, and interaction partners. Produced via heterologous expression systems (e.g., E. coli, mammalian cells), the recombinant protein is purified using affinity tags (e.g., His-tag) and validated via functional assays, such as vesicular transport experiments or fluorescence-based uptake assays. Its applications span structural biology, drug discovery, and mechanistic studies of glycosylation-related pathways.
Research on SLC35F3 may advance understanding of glycosylation defects in diseases and inspire therapeutic strategies targeting transporter activity. However, challenges persist in confirming its endogenous substrates and regulatory mechanisms, necessitating further interdisciplinary studies.
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