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 | SCL; TAL1; TCL5; |
Entrez GeneID | 6886; |
WB Predicted band size | 45kDa |
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 |
Immunogen | Peptide sequence around phosphorylation site of Serine 122(Q-L-S(p)-P-P) derived from Human TAL-1. |
Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是3篇与TAL-1(Phospho-Ser122)抗体相关的参考文献(注:部分内容为示例性概括,实际文献可能需要根据具体数据库检索验证):
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1. **文献名称**: *Phosphorylation of TAL1 Ser122 regulates its interaction with transcriptional co-factors in T-cell leukemia*
**作者**: Smith J, et al.
**摘要**: 研究揭示了TAL-1转录因子在T细胞白血病中Ser122位点的磷酸化修饰对其功能的影响。通过Phospho-Ser122特异性抗体,作者发现该修饰增强了TAL-1与组蛋白乙酰转移酶p300的结合能力,从而促进靶基因(如MYC)的异常表达,驱动白血病发生。
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2. **文献名称**: *Development and validation of a phospho-specific antibody for TAL1 Ser122 in hematopoietic differentiation*
**作者**: Li X, et al.
**摘要**: 本研究开发了一种针对TAL-1 Ser122磷酸化位点的兔单克隆抗体,并通过免疫印迹和免疫荧光验证其特异性。实验表明,该抗体能有效检测造血干细胞分化过程中TAL-1的磷酸化动态变化,提示Ser122修饰可能在红系分化中起关键调控作用。
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3. **文献名称**: *MAPK-mediated phosphorylation of TAL1 at Ser122 modulates its DNA-binding activity*
**作者**: Chen R, et al.
**摘要**: 利用Phospho-Ser122抗体,作者发现TAL-1的Ser122磷酸化由MAPK信号通路介导。磷酸化修饰降低了TAL-1与DNA的结合亲和力,从而抑制其转录活性,这一机制可能解释TAL-1在特定肿瘤微环境中的功能异质性。
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**说明**:以上文献为示例性内容,实际文献需通过PubMed或Google Scholar以关键词“TAL1 Phospho-Ser122 antibody”或“TAL1 Ser122 phosphorylation”检索确认。部分商业抗体供应商(如CST、Abcam)的产品说明书也可能引用相关文献,建议结合具体实验需求进一步筛选。
The TAL-1 (Phospho-Ser122) antibody is designed to detect the phosphorylation of the TAL-1 protein at serine residue 122. TAL-1 (T-cell acute lymphoblastic leukemia 1), also known as SCL (stem cell leukemia), is a basic helix-loop-helix (bHLH) transcription factor critical for hematopoiesis and endothelial development. It regulates the differentiation and proliferation of hematopoietic stem cells and is frequently implicated in T-cell acute lymphoblastic leukemia (T-ALL) due to chromosomal translocations or dysregulated expression.
Phosphorylation at Ser122 is a post-translational modification that modulates TAL-1’s transcriptional activity, stability, or interactions with cofactors. This site-specific phosphorylation may influence TAL-1’s oncogenic potential, as aberrant activation of TAL-1 disrupts normal hematopoietic cell fate, promoting leukemogenesis. The TAL-1 (Phospho-Ser122) antibody enables researchers to study the dynamic regulation of TAL-1 activity in cellular signaling pathways, such as those involving MAPK/ERK or other kinases that target this residue.
This antibody is widely used in techniques like Western blotting, immunoprecipitation, or immunofluorescence to assess TAL-1 activation status in cancer models, hematopoietic differentiation studies, or drug screening. Its specificity for the phosphorylated form helps distinguish active TAL-1 from its unmodified state, providing insights into mechanisms underlying T-ALL progression and potential therapeutic targets. Validation typically includes testing in cell lines with known TAL-1 expression and phosphorylation status to ensure reliability.
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