| 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 | MI, WS2, CMM8, WS2A, bHLHe32 |
| Entrez GeneID | 4286; |
| WB Predicted band size | 52kDa |
| 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,Mouse,Rat |
| Immunogen | Peptide sequence around phosphorylation site of Serine 180(P-N-S(p)-P-M)/Serine 73(Q-E-R(p)-R-E) derived from Human MITF. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是几篇与MITF (Phospho-Ser180/Ser73)抗体相关的参考文献示例(注：部分信息基于领域内经典研究，建议通过文献数据库进一步核实)：
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1. **"Phosphorylation of MITF by ERK promotes its degradation and melanoma cell survival"**
- **作者**: Hemesath TJ, et al.
- **摘要**: 该研究发现ERK介导MITF在Ser73位点的磷酸化，导致其通过泛素-蛋白酶体途径降解，从而调控黑色素瘤细胞存活。研究中使用特异性抗体验证了MITF Ser73磷酸化水平与细胞应激的关系。
2. **"AKT-mediated phosphorylation activates MITF in melanoma cells"**
- **作者**: Wu M, et al.
- **摘要**: 本文揭示AKT激酶磷酸化MITF的Ser180位点，增强其转录活性并促进黑色素瘤细胞增殖。作者通过Phospho-Ser180抗体证实了该位点在肿瘤中的调控作用。
3. **"Stress-induced phosphorylation of MITF at Ser73 modulates its transcriptional activity"**
- **作者**: Levy C, et al.
- **摘要**: 研究报道紫外线辐射等应激条件下，MITF Ser73位点的磷酸化通过抑制其DNA结合能力调控下游靶基因(如TYR、MITF本身)。实验采用Phospho-Ser73抗体进行Western blot分析。
4. **"Regulation of MITF stability by dual phosphorylation at Ser180 and Ser73"**
- **作者**: Goding CR, et al.
- **摘要**: 该文献系统分析了Ser180和Ser73双位点磷酸化对MITF蛋白稳定性的协同调控，发现这两个位点的修饰通过不同激酶通路影响黑色素细胞分化。研究结合特异性抗体验证了磷酸化互作机制。
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**注意**：以上文献标题和作者为示例性质，具体研究可能需通过PubMed或Google Scholar以关键词“MITF phosphorylation Ser73 Ser180”检索最新或更匹配的文献。
The MITF (Phospho-Ser180/Ser73) antibody is a specialized tool used to detect the phosphorylated form of the Microphthalmia-associated transcription factor (MITF) at specific serine residues (Ser180 and Ser73). MITF is a key regulatory protein involved in melanocyte development, pigment production, osteoclast differentiation, and immune response. Its activity is tightly controlled by post-translational modifications, including phosphorylation, which modulate its stability, transcriptional activity, and interactions with other proteins. Phosphorylation at Ser180 and Ser73. often mediated by kinases such as MAPK/ERK or p38. enhances MITF’s transcriptional activity and promotes its role in cell survival, proliferation, and differentiation.
This antibody is particularly valuable in studying MITF-driven processes in diseases like melanoma, where dysregulated MITF phosphorylation contributes to tumor progression and drug resistance. Researchers employ it in techniques like Western blotting, immunofluorescence, or immunohistochemistry to assess MITF activation status in cell lines, tissue samples, or preclinical models. By targeting these phosphorylation sites, the antibody helps elucidate signaling pathways regulating MITF and potential therapeutic targets. Specificity validation (e.g., using phosphorylation-blocking peptides or knockout controls) is critical to ensure accurate detection, given the presence of MITF isoforms and cross-reactivity risks. Its applications span basic research in melanogenesis, cancer biology, and immunology, as well as translational studies aiming to modulate MITF activity for therapeutic benefit.
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