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 | Signal transducer and activator of transcription 5B; STA5B; STAT5; transcription factor STAT5B; |
Entrez GeneID | 20850; |
WB Predicted band size | 90kDa |
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 | Peptide sequence around phosphorylation site of serine725/730(A-P-S(p)-P-V) derived from Human STAT5A/B. |
Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于STAT5A/B (Phospho-Ser725/730)抗体的3篇参考文献的简要总结:
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1. **文献名称**:*STAT5 requires the serine site for leukemogenesis but not for normal hematopoiesis*
**作者**:Hoelbl et al.
**摘要**:研究通过STAT5A/B Ser725/730磷酸化位点突变小鼠模型,发现该位点的磷酸化对白血病发展至关重要,但对正常造血功能无显著影响。实验中利用Phospho-Ser725/730抗体验证了STAT5在白血病中的异常激活机制。
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2. **文献名称**:*Prolactin-induced phosphorylation of STAT5A/B at Ser725/730 regulates its transcriptional activity*
**作者**:Yamashita et al.
**摘要**:探讨催乳素信号通路中STAT5A/B Ser725/730位点的磷酸化调控机制,使用特异性抗体证实该修饰增强STAT5的核转位及靶基因转录活性,揭示了激素依赖性STAT5激活的新模式。
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3. **文献名称**:*Differential roles of STAT5 phosphorylation sites in regulating myeloid leukemia progression*
**作者**:Moriggl et al.
**摘要**:通过功能实验和Phospho-Ser725/730抗体的免疫印迹分析,证明STAT5 Ser725/730磷酸化在髓系白血病中驱动细胞增殖和存活,且与JAK-STAT通路抑制剂耐药性相关。
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**备注**:若需更详细的文献信息(期刊、年份等),可进一步补充。建议通过PubMed或Web of Science以关键词“STAT5A/B Ser725/730 phosphorylation”检索最新研究。
The STAT5A and STAT5B proteins are members of the Signal Transducer and Activator of Transcription (STAT) family, which play critical roles in mediating cellular responses to cytokines, growth factors, and hormones. Upon activation by receptor-associated kinases (e.g., JAK kinases), STAT5A/B undergo tyrosine phosphorylation, dimerize, and translocate to the nucleus to regulate gene expression. In addition to tyrosine phosphorylation, serine phosphorylation at specific residues, such as Ser725 in STAT5A and Ser730 in STAT5B, has been identified as a regulatory mechanism influencing transcriptional activity, protein stability, or interaction with co-regulators. Phosphorylation at these sites is associated with distinct signaling contexts, including prolonged cytokine stimulation or alternative kinase pathways.
Antibodies targeting STAT5A/B phosphorylated at Ser725/730 are essential tools for studying the activation dynamics and functional roles of these post-translational modifications. They enable the detection of serine-phosphorylated STAT5 isoforms in techniques like Western blotting, immunofluorescence, or immunoprecipitation, helping researchers dissect context-specific signaling mechanisms. Such antibodies are particularly valuable in cancer research, as aberrant STAT5 activation is linked to tumor progression, immune evasion, and therapy resistance. They also aid in exploring physiological processes like hematopoiesis, lactation, and T-cell differentiation. Validation of these antibodies typically includes testing in knockout models or phosphatase-treated samples to confirm specificity for the phosphorylated epitope.
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