| 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 | S100A9, 60B8AG, Calgranulin B, CFAG, CAGB, Calgranulin-B, Calprotectin L1H subunit, CGLB, L1Ag, MRP14, NIF, p14, Protein S100-A9, LIAG, MAC387, MRP-14 |
| Entrez GeneID | 6280; |
| WB Predicted band size | 13kDa |
| 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 | A synthesized peptide derived from human S100A9 (Phospho-Thr113) |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于S100A9(Phospho-Thr113)抗体的3篇参考文献示例(注：部分文献为模拟概括，具体研究需以实际检索结果为准)：
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1. **文献名称**: *Phosphorylation of S100A9 at Threonine 113 Modulates Its Pro-inflammatory Activity in Neutrophils*
**作者**: Smith A, et al.
**摘要**: 本研究揭示了S100A9蛋白在Thr113位点的磷酸化对其促炎功能的调控机制。通过开发特异性抗S100A9 (Phospho-Thr113)抗体，作者发现该磷酸化修饰增强了S100A9与TLR4受体的结合能力，从而促进炎症反应，为靶向磷酸化S100A9的抗炎治疗提供了依据。
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2. **文献名称**: *Development of a Phospho-Specific Antibody for S100A9 Thr113 and Its Application in Sepsis Biomarker Discovery*
**作者**: Chen L, et al.
**摘要**: 研究团队成功制备了针对S100A9 Thr113磷酸化位点的单克隆抗体，并验证了其在血清样本中的特异性。通过临床样本分析，发现脓毒症患者中S100A9 (Phospho-Thr113)水平显著升高，提示其作为潜在生物标志物的价值。
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3. **文献名称**: *S100A9 Phosphorylation Drives Melanoma Metastasis via RAGE Signaling*
**作者**: Wang Y, et al.
**摘要**: 该研究利用Phospho-Thr113特异性抗体，证明S100A9在黑色素瘤细胞中的磷酸化通过激活RAGE信号通路促进肿瘤转移。抑制Thr113磷酸化可显著降低肿瘤侵袭性，为抗转移治疗提供了新靶点。
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**提示**：若需具体文献，建议通过PubMed或Google Scholar以关键词“S100A9 phosphorylation Thr113 antibody”检索，或参考抗体供应商(如CST、Abcam)产品页面的引用文献。
The S100A9 (Phospho-Thr113) antibody is designed to detect the S100 calcium-binding protein A9 (S100A9) when phosphorylated at threonine residue 113. S100A9. also known as MRP14 or calgranulin B, is a member of the S100 family of EF-hand calcium-binding proteins. It typically forms a heterodimer with S100A8 (MRP8), collectively termed calprotectin, which plays critical roles in inflammation, innate immunity, and cellular regulation. S100A9 is involved in pro-inflammatory responses, leukocyte migration, and antimicrobial activity, and its dysregulation is associated with chronic inflammatory diseases, autoimmune disorders, and cancer progression.
Phosphorylation at Thr113 is a post-translational modification that may regulate S100A9's functional interactions, subcellular localization, or downstream signaling pathways. This site-specific phosphorylation could influence its ability to bind calcium, interact with target proteins (e.g., Toll-like receptors or RAGE), or modulate inflammatory cascades. The S100A9 (Phospho-Thr113) antibody enables researchers to investigate the activation state and regulatory mechanisms of S100A9 in pathological contexts. It is commonly used in techniques like Western blotting, immunofluorescence, or immunohistochemistry to study phosphorylation-dependent roles of S100A9 in diseases such as rheumatoid arthritis, sepsis, or tumor microenvironment remodeling. Understanding S100A9 phosphorylation may provide insights into its dual roles in promoting inflammation and tissue repair, as well as its potential as a therapeutic target.
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