| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | Prominin-1, Antigen AC133, Prominin-like protein 1, CD133, PROM1, PROML1 |
| Entrez GeneID | 8842 |
| WB Predicted band size | 97.2kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human |
| Immunogen | This Phospho-CD133-pY828 antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding Y828 of human CD133. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于Phospho-CD133-pY828抗体的3篇虚构参考文献示例(基于常见研究主题，非真实文献)：
1. **文献名称**：*Phosphorylation of CD133 at Tyrosine 828 Regulates Cancer Stem Cell Properties in Glioblastoma*
**作者**：Zhang L. et al.
**摘要**：研究揭示了CD133在酪氨酸828位点(Y828)的磷酸化通过激活PI3K/Akt信号通路增强胶质母细胞瘤干细胞的自我更新和耐药性，Phospho-CD133-pY828抗体被用于检测磷酸化水平及其与患者预后的相关性。
2. **文献名称**：*Tyrosine 828 Phosphorylation Modulates CD133 Interaction with Src Kinase in Colorectal Cancer Metastasis*
**作者**：Wang Y. et al.
**摘要**：该研究利用Phospho-CD133-pY828抗体证明，Y828磷酸化促进CD133与Src激酶的结合，进而增强结直肠癌细胞迁移和侵袭能力，提示其作为转移治疗靶点的潜力。
3. **文献名称**：*Targeting Phosphorylated CD133 (pY828) Enhances Chemosensitivity in Hepatocellular Carcinoma*
**作者**：Chen H. et al.
**摘要**：通过抑制CD133 Y828磷酸化(使用特异性抗体验证)，可降低肝癌干细胞对化疗的耐药性，机制涉及Wnt/β-catenin信号通路的下调，为联合治疗提供新策略。
注：以上内容为示例性虚构文献，实际研究中请通过PubMed或Google Scholar检索真实文献。
The Phospho-CD133-pY828 antibody is a specialized tool used to detect the phosphorylated form of CD133 (Prominin-1) at tyrosine residue 828. CD133. a transmembrane glycoprotein, is a well-established marker of stem and progenitor cells, particularly in cancer stem cells (CSCs), where it is linked to self-renewal, tumor initiation, and therapy resistance. Tyrosine phosphorylation at position 828 (Y828) is a post-translational modification implicated in regulating CD133's functional interactions, signaling pathways, and cellular localization. This phosphorylation event may influence CD133’s role in modulating intracellular signaling cascades, such as PI3K/AKT or MAPK pathways, which are critical for maintaining stemness, survival, and metastatic potential in malignancies.
The antibody is commonly employed in research to study the activation status and biological roles of CD133 in contexts like tumor progression, metastasis, and therapeutic resistance. It enables specific detection of phosphorylated CD133 via techniques like Western blotting, immunofluorescence, or immunohistochemistry, aiding in the identification of activated CSC populations. Dysregulation of CD133 phosphorylation has been associated with aggressive cancer phenotypes, making this antibody a valuable tool for exploring mechanisms underlying CSC-driven tumor recurrence and targeted therapy development. Its applications extend to elucidating phosphorylation-dependent protein interactions and biomarker discovery in oncology and stem cell biology.
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