| 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 | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 1/40000 | Human,Mouse,Rat |
| Aliases | PBK; TOPK; Lymphokine-activated killer T-cell-originated protein kinase; Cancer/testis antigen 84; CT84; MAPKK-like protein kinase; Nori-3; PDZ-binding kinase; Spermatogenesis-related protein kinase; SPK; T-LAK cell-originated protein kinas |
| Entrez GeneID | 55872; |
| WB Predicted band size | 36kDa |
| 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 | Synthesized peptide derived from human PBK around the phosphorylation site of T9. |
| 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PBK (Phospho-Thr9)抗体的3篇参考文献示例(注：文献为虚构示例，实际引用需核实)：
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1. **文献名称**: *"Phosphorylation of PBK/TOPK at Thr9 by CDK1 Promotes Mitotic Progression and Cancer Cell Survival"*
**作者**: Zhang Y, Li Q, et al.
**摘要**: 研究揭示了PBK的Thr9位点磷酸化由CDK1调控，并利用Phospho-Thr9特异性抗体证实其在细胞有丝分裂中的作用。结果显示，抑制该磷酸化会导致癌细胞凋亡，提示其作为潜在治疗靶点。
2. **文献名称**: *"Development of a Phospho-Specific Antibody for PBK Thr9 and Its Application in Glioblastoma Studies"*
**作者**: Smith J, Brown K, et al.
**摘要**: 本文报道了一种针对PBK Thr9磷酸化位点的单克隆抗体的开发，并通过质谱和免疫印迹验证其特异性。该抗体成功用于胶质母细胞瘤组织样本的检测，显示磷酸化水平与肿瘤分级相关。
3. **文献名称**: *"TOPK Thr9 Phosphorylation Mediates DNA Damage Response via Interaction with BRCA1"*
**作者**: Chen L, Wang H, et al.
**摘要**: 研究发现PBK的Thr9磷酸化在DNA损伤修复中与BRCA1蛋白互作，使用Phospho-Thr9抗体进行免疫沉淀实验，证实其调控同源重组修复的分子机制。
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**注意**：以上文献为示例，实际研究中请通过PubMed、Google Scholar或抗体厂商(如CST、Abcam)提供的引用文献核实具体内容。若需真实文献，建议检索关键词“PBK Thr9 phosphorylation antibody”或联系抗体供应商获取相关引用。
**Background of PBK (Phospho-Thr9) Antibody**
PBK (PDZ-binding kinase), also known as TOPK (T-LAK cell-originated protein kinase), is a serine/threonine kinase belonging to the mitogen-activated protein kinase (MAPK) family. It plays critical roles in cell cycle regulation, DNA damage response, and tumorigenesis. PBK is notably overexpressed in various cancers, including breast, colorectal, and glioblastoma, where it promotes proliferation, suppresses apoptosis, and enhances metastatic potential.
Phosphorylation at specific residues regulates PBK’s activity. The Thr9 phosphorylation site (Phospho-Thr9) is associated with its kinase activation and interaction with downstream targets, such as histone H3 and p38 MAPK. This post-translational modification is crucial for PBK’s function in mitotic progression, particularly during the G2/M phase transition, and its role in sustaining genomic stability.
The PBK (Phospho-Thr9) antibody is a specialized tool designed to detect PBK phosphorylated at Thr9. It enables researchers to study the activation status and functional dynamics of PBK in cellular signaling pathways. Applications include Western blotting, immunohistochemistry, and immunofluorescence, aiding in the investigation of PBK’s oncogenic mechanisms, therapeutic targeting, and its correlation with cancer prognosis. Validated for specificity, this antibody helps elucidate PBK’s contribution to tumor progression and its potential as a biomarker or therapeutic target in oncology research.
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