WB | 咨询技术 | Human,Mouse,Rat |
IF | 咨询技术 | Human,Mouse,Rat |
IHC | 1/100-1/300 | Human,Mouse,Rat |
ICC | 1/200-1/1000 | Human,Mouse,Rat |
FCM | 咨询技术 | Human,Mouse,Rat |
Elisa | 1/10000 | Human,Mouse,Rat |
Aliases | PLA2G4A; CPLA2; PLA2G4; Cytosolic phospholipase A2; cPLA2; Phospholipase A2 group IVA |
Entrez GeneID | 5321; |
WB Predicted band size | 110kDa |
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 | Synthesized peptide derived from human cPLA2 around the phosphorylation site of S505. |
Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
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以下是关于 **cPLA2 (Phospho-Ser505) 抗体**的参考文献,包含文献名称、作者及摘要内容概括:
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1. **"Phosphorylation and activation of cytosolic phospholipase A2 by mitogen-activated protein kinase in human monocytes"**
*Clark et al. (1995), Journal of Biological Chemistry*
摘要:研究报道cPLA2在Ser505位点被MAPK磷酸化,该修饰增强其与膜磷脂的结合能力,促进花生四烯酸释放,为炎症信号传导的关键机制。
2. **"Role of phosphorylation sites in the regulation of cytosolic phospholipase A2 activity and arachidonic acid release"**
*Leslie & Channon (1996), Biochimica et Biophysica Acta*
摘要:通过突变Ser505位点验证其磷酸化对cPLA2酶活性的必要性,并利用Phospho-Ser505抗体证明其在细胞因子刺激下的磷酸化动力学。
3. **"Regulation of cytosolic phospholipase A2 activation by phosphorylation in mouse macrophages"**
*Gijón et al. (2000), Journal of Immunology*
摘要:在小鼠巨噬细胞中,利用Phospho-Ser505抗体检测LPS诱导的cPLA2磷酸化,阐明其与炎症介质(如前列腺素)产生的关联。
4. **"Selective phosphorylation of cytosolic phospholipase A2 in neurological disorders"**
*Hegen et al. (2003), Journal of Neurochemistry*
摘要:通过免疫印迹分析脑缺血模型中的cPLA2磷酸化水平,揭示Ser505磷酸化在神经炎症及神经元损伤中的作用。
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这些文献均涉及cPLA2在Ser505位点的磷酸化机制及其生物学意义,其中抗体被用于检测磷酸化状态并关联酶活性或疾病模型。
The cPLA2 (Phospho-Ser505) antibody detects the phosphorylated form of cytosolic phospholipase A2-alpha (cPLA2α) at serine 505. a post-translational modification critical for its enzymatic activation. cPLA2α, encoded by the PLA2G4A gene, is a calcium-dependent phospholipase that selectively hydrolyzes membrane phospholipids to release arachidonic acid (AA), a precursor for pro-inflammatory lipid mediators like prostaglandins and leukotrienes. Phosphorylation at Ser505. mediated by mitogen-activated protein kinases (MAPKs) such as ERK1/2 during cellular stimulation (e.g., by cytokines, growth factors, or stress signals), enhances cPLA2α’s translocation to membranes and catalytic activity. This modification is a key regulatory step in inflammatory signaling pathways.
The cPLA2 (Phospho-Ser505) antibody is widely used in research to study cPLA2α activation dynamics in conditions like inflammation, cancer, and neurodegenerative diseases. It enables the detection of phosphorylated cPLA2α via techniques like Western blotting, immunohistochemistry, or immunofluorescence, helping elucidate its role in cellular responses. Dysregulated cPLA2α activity is linked to pathological processes, making this antibody a valuable tool for probing disease mechanisms or evaluating therapeutic interventions targeting AA metabolism. Specificity validation (e.g., using phosphorylation-blocking peptides or knockout controls) is essential to ensure accurate interpretation of experimental results.
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