| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PROM1 |
| Uniprot No | O43490-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-856aa |
| 氨基酸序列 | MALVLGSLLLLGLCGNSFSGGQPSSTDAPKAWNYELPATNYETQDSHKAG PIGILFELVHIFLYVVQPRDFPEDTLRKFLQKAYESKIDYDKIVYYEAGI ILCCVLGLLFIILMPLVGYFFCMCRCCNKCGGEMHQRQKENGPFLRKCFA ISLLVICIIISIGIFYGFVANHQVRTRIKRSRKLADSNFKDLRTLLNETP EQIKYILAQYNTTKDKAFTDLNSINSVLGGGILDRLRPNIIPVLDEIKSM ATAIKETKEALENMNSTLKSLHQQSTQLSSSLTSVKTSLRSSLNDPLCLV HPSSETCNSIRLSLSQLNSNPELRQLPPVDAELDNVNNVLRTDLDGLVQQ GYQSLNDIPDRVQRQTTTVVAGIKRVLNSIGSDIDNVTQRLPIQDILSAF SVYVNNTESYIHRNLPTLEEYDSYWWLGGLVICSLLTLIVIFYYLGLLCG VCGYDRHATPTTRGCVSNTGGVFLMVGVGLSFLFCWILMIIVVLTFVFGA NVEKLICEPYTSKELFRVLDTPYLLNEDWEYYLSGKLFNKSKMKLTFEQV YSDCKKNRGTYGTLHLQNSFNISEHLNINEHTGSISSELESLKVNLNIFL LGAAGRKNLQDFAACGIDRMNYDSYLAQTGKSPAGVNLLSFAYDLEAKAN SLPPGNLRNSLKRDAQTIKTIHQQRVLPIEQSLSTLYQSVKILQRTGNGL LERVTRILASLDFAQNFITNNTSSVIIEETKKYGRTIIGYFEHYLQWIEF SISEKVASCKPVATALDTAVDVFLCSYIIDPLNLFWFGIGKATVFLLPAL IFAVKLAKYYRRMDSEDVYDDVETIPMKNMENGNNGYHKDHVYGIHNPVM TSPSQH |
| 预测分子量 | 123 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3篇与PROM1重组蛋白相关的文献摘要信息：
1. **《Recombinant PROM1 protein enhances stem cell self-renewal in vitro》**
- 作者：Zhang Y, et al.
- 摘要：研究通过大肠杆菌系统表达PROM1重组蛋白，证实其可通过激活Wnt/β-catenin信号通路促进间充质干细胞的自我更新能力。
2. **《Structural characterization of human PROM1 extracellular domain》**
- 作者：Lee S, Kim JH.
- 摘要：利用哺乳动物细胞表达系统获得高纯度PROM1胞外段重组蛋白，通过冷冻电镜解析其三维结构，揭示其与胆固醇结合的分子机制。
3. **《PROM1-targeted recombinant protein inhibits tumor growth in glioblastoma models》**
- 作者：Wang X, et al.
- 摘要：开发基于PROM1抗原表位的重组融合蛋白，在胶质母细胞瘤小鼠模型中显示特异性靶向肿瘤干细胞并抑制肿瘤增殖。
注：以上为示例性文献，实际引用需核对具体论文数据。建议通过PubMed或Web of Science以“PROM1 recombinant protein”为关键词检索最新研究。
PROM1 (Prominin-1), also known as CD133. is a transmembrane glycoprotein encoded by the PROM1 gene in humans. First identified in 1997. it is characterized by five transmembrane domains and two large extracellular loops, which contribute to its role in membrane organization and cellular signaling. PROM1 is widely recognized as a marker of stem and progenitor cells, particularly in epithelial, hematopoietic, and neural tissues. Its expression is associated with self-renewal capacity, making it a key focus in cancer research, as tumor-initiating "cancer stem cells" (CSCs) often overexpress PROM1.
Recombinant PROM1 protein is produced using engineered expression systems (e.g., mammalian cells or E. coli) to enable functional studies. This purified protein retains structural and biological properties of native PROM1. allowing researchers to investigate its interactions with membrane cholesterol, involvement in extracellular vesicle formation, and regulatory roles in signaling pathways like Wnt/β-catenin. Recombinant forms are crucial for developing antibodies, diagnostic tools, and therapeutic strategies targeting PROM1-positive cells.
In disease contexts, PROM1 overexpression correlates with poor prognosis in glioblastoma, colorectal cancer, and other malignancies. Its recombinant version facilitates drug screening for CSC-targeted therapies and vaccine development. Additionally, PROM1 mutations are linked to inherited retinal disorders (e.g., Stargardt disease), driving research into gene therapies. Challenges remain in characterizing post-translational modifications (e.g., glycosylation) that affect its function, though recent advances in structural biology (cryo-EM studies) and optimized recombinant production systems are accelerating mechanistic insights. Current applications span regenerative medicine, anti-cancer drug discovery, and biomarker development.
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