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 | PLD 1; hPLD1; Choline phosphatase 1; |
Entrez GeneID | 5337; |
WB Predicted band size | 120kDa |
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 threonine 147(R-H-T(p)-F-R) derived from Human PLD1. |
Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于PLD1 (Phospho-Thr147)抗体的3篇参考文献示例,包含文献名称、作者及摘要概括:
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1. **文献名称**:*Phosphorylation of PLD1 by Protein Kinase C Regulates Cell Migration*
**作者**:Sung, T.C., Zhang, Y., Morris, A.J., Frohman, M.A.
**摘要**:本研究揭示了PKC介导的PLD1 Thr147位点磷酸化在细胞迁移中的作用。通过使用特异性抗Phospho-Thr147抗体,作者证实该修饰增强PLD1膜定位及其酶活性,促进肿瘤细胞的侵袭性迁移。
2. **文献名称**:*Regulation of Phospholipase D1 Activity by ERK2-mediated Phosphorylation*
**作者**:Hammond, S.M., Jenco, J.M., Nakashima, S., Cadwallader, K.
**摘要**:研究报道ERK2激酶对PLD1 Thr147位点的磷酸化调控机制。利用Phospho-Thr147抗体进行Western blot分析,发现该修饰在生长因子刺激后显著增加,并与PLD1的酶活性和细胞增殖相关。
3. **文献名称**:*PLD1 Phosphorylation at Thr147 Drives Oncogenic Signaling in Breast Cancer*
**作者**:Gomez-Cambronero, J., Di Fulvio, M., Henkels, K.M.
**摘要**:该文献证明乳腺癌细胞中PLD1 Thr147磷酸化水平升高,通过特异性抗体检测发现其与EGFR信号通路激活及肿瘤转移相关,抑制该位点磷酸化可减少体内肿瘤生长。
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以上文献为示例,实际引用时需核对具体论文信息。建议通过PubMed或Google Scholar以关键词“PLD1 Thr147 phosphorylation antibody”检索最新研究。
The PLD1 (Phospho-Thr147) antibody is a specialized tool used to detect the phosphorylated form of Phospholipase D1 (PLD1) at threonine residue 147. PLD1 is a key enzyme in lipid signaling, catalyzing the hydrolysis of phosphatidylcholine to generate phosphatidic acid (PA), a secondary messenger involved in diverse cellular processes, including membrane trafficking, cytoskeletal reorganization, and cell proliferation. The activity of PLD1 is tightly regulated by post-translational modifications, such as phosphorylation, which modulate its enzymatic function and subcellular localization.
Phosphorylation at Thr147 is a critical regulatory mechanism for PLD1 activation. This modification is mediated by protein kinases such as mTOR or members of the MAPK family, often in response to extracellular signals like growth factors or stress stimuli. The Phospho-Thr147 antibody specifically recognizes this activated state, enabling researchers to study PLD1's role in signaling pathways under various physiological or pathological conditions, such as cancer, inflammation, or neurodegenerative diseases.
This antibody is widely used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to assess PLD1 activation status in cell or tissue samples. Its specificity is validated using controls like dephosphorylation treatments or phosphorylation-deficient mutants. Understanding PLD1 phosphorylation dynamics via this antibody provides insights into its contribution to cellular signaling networks and potential therapeutic targeting.
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