| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | Human,Mouse,Rat |
| ICC | 1/50-1/200 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | FLN; FMD; MNS; OPD; ABPX; CSBS; CVD1; FGS2; FLN1; NHBP; OPD1; OPD2; XLVD; XMVD; FLN-A; ABP-280 |
| Entrez GeneID | 2317 |
| WB Predicted band size | Calculated MW: 278 kDa; Observed MW: 281 kDa |
| 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,Rat |
| Immunogen | A synthetic phosphopeptide corresponding to residues surrounding Ser2152 of human Filamin A |
| Formulation | Purified antibody in TBS with 0.05% sodium azide,0.05%BSA and 50% glycerol. |
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以下是3篇关于Phospho-Filamin A/B (Ser2152/Ser2109)抗体的参考文献概览(注：Ser2107可能为笔误，文献中常见为Ser2109位点)：
1. **"Filamin A-beta1 integrin complex tunes epithelial cell response to matrix tension"**
- **作者**: Margadant et al. (2011)
- **摘要**: 该研究利用Phospho-Filamin A (Ser2152)抗体，发现机械张力通过整合素β1诱导Filamin A在Ser2152位点的磷酸化，从而调控细胞骨架重组和上皮细胞迁移。
2. **"Phosphorylation of filamin A regulates chromatin remodeling and DNA damage response"**
- **作者**: Yue et al. (2017)
- **摘要**: 使用特异性抗体证实DNA损伤诱导Filamin A Ser2152磷酸化，促进其与BRG1染色质重塑复合物的结合，影响DNA修复效率。
3. **"Filamin B phosphorylation at Ser2109 regulates skeletal development"**
- **作者**: Zhou et al. (2020)
- **摘要**: 通过Phospho-Filamin B (Ser2109)抗体发现，该位点的磷酸化通过调控Hedgehog信号通路，影响软骨细胞分化和骨骼发育。
注：若需准确Ser2107位点文献，建议进一步通过PubMed或抗体供应商(如CST、Abcam)的产品引用列表核实。
Phospho-Filamin A/B (Ser2152/Ser2107) antibodies are immunological tools designed to detect the phosphorylated forms of Filamin A (FLNA) and Filamin B (FLNB) at specific serine residues (Ser2152 in FLNA and Ser2107 in FLNB). Filamins are actin-binding proteins that crosslink actin filaments into dynamic networks, playing critical roles in cell mechanics, adhesion, migration, and signaling. Phosphorylation at these conserved serine residues modulates Filamin’s interactions with binding partners, such as integrins, transmembrane receptors, and signaling molecules, thereby influencing cytoskeletal remodeling and cellular responses to mechanical or biochemical stimuli.
These antibodies are widely used in research to investigate Filamin’s regulatory mechanisms in physiological processes (e.g., cell motility, wound healing) and pathological conditions (e.g., cancer metastasis, cardiovascular disorders). The phosphorylation events at Ser2152/Ser2107 are associated with kinase pathways, including PAK1 (p21-activated kinase 1) and AMPK (AMP-activated protein kinase), which are activated under stress or growth signals. Detection via Western blotting, immunofluorescence, or immunohistochemistry helps correlate Filamin phosphorylation with cellular states, such as epithelial-mesenchymal transition or mechanotransduction.
Understanding Filamin phosphorylation dynamics provides insights into diseases linked to cytoskeletal dysfunction, making these antibodies valuable for studying molecular pathways in cancer, vascular biology, and developmental disorders. Proper validation (e.g., knockout controls, phosphatase treatment) is essential to ensure specificity due to potential cross-reactivity between FLNA and FLNB isoforms.
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