| 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 | BLK, Blk kinase, B lymphocyte kinase, B lymphoid tyrosine kinase, MODY11, Protein kinase blk, Protein tyrosine kinase blk, B lymphoid kinase, p55-Blk, Tyrosine-protein kinase Blk |
| Entrez GeneID | 640; |
| WB Predicted band size | 58kDa |
| 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 | A synthesized peptide derived from human BLK (Phospho-Tyr389) |
| Formulation | Purified antibody in PBS with 0.05% sodium azide and 30% glycerol. |
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以下是关于 BLK (Phospho-Tyr389) 抗体的虚构参考文献示例，内容基于合理推测：
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1. **Title**: *Phosphorylation of BLK at Tyr389 regulates B-cell receptor signaling in autoimmune pathogenesis*
**Author**: Smith et al.
**Summary**: 本研究利用 BLK (Phospho-Tyr389) 特异性抗体，揭示了 BLK 在 B 细胞受体(BCR)信号中的激活机制。作者发现，Tyr389 磷酸化是 BLK 激酶活性的关键调节位点，其异常激活与系统性红斑狼疮(SLE)患者 B 细胞的过度反应相关。
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2. **Title**: *Structural insights into BLK activation through tyrosine phosphorylation at residue 389*
**Author**: Zhang et al.
**Summary**: 通过 X 射线晶体学和磷酸化特异性抗体检测，本研究解析了 BLK 在 Tyr389 磷酸化后的构象变化，阐明其如何促进激酶结构域的开放状态，从而增强下游信号转导。研究为靶向 BLK 的药物设计提供了结构基础。
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3. **Title**: *BLK tyrosine 389 phosphorylation as a biomarker in rheumatoid arthritis*
**Author**: Tanaka et al.
**Summary**: 通过 ELISA 和 Western blot 结合 Phospho-Tyr389 抗体，研究发现类风湿性关节炎(RA)患者外周血 B 细胞中 BLK 的 Tyr389 磷酸化水平显著升高，提示其可作为疾病活动性的潜在生物标志物。
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4. **Title**: *A small-molecule inhibitor targeting BLK phosphorylation suppresses B-cell lymphoma progression*
**Author**: Johnson et al.
**Summary**: 本研究开发了一种靶向 BLK Tyr389 磷酸化的小分子抑制剂，并利用 Phospho-Tyr389 抗体验证其抑制效果。实验表明，该抑制剂可阻断 BLK 介导的 NF-κB 通路活化，显著延缓 B 细胞淋巴瘤的进展。
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注：以上文献为示例性内容，实际引用时需检索真实数据库(如 PubMed)获取准确信息。
The BLK (B lymphocyte kinase) protein is a member of the Src family of tyrosine kinases, primarily expressed in B cells and involved in B-cell receptor (BCR) signaling. Phosphorylation at Tyr389 in the activation loop of BLK is critical for its enzymatic activity, serving as a regulatory switch to modulate downstream signaling cascades. This phosphorylation event stabilizes the active conformation of the kinase, enabling interactions with substrates and adaptor proteins to propagate signals that influence B-cell development, differentiation, and immune responses.
Antibodies targeting BLK phosphorylated at Tyr389 (Phospho-Tyr389) are essential tools for studying the activation status of BLK in physiological and pathological contexts. They are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to assess BLK activation dynamics in response to stimuli such as antigen engagement or cytokine signaling. Dysregulation of BLK activity has been implicated in autoimmune disorders (e.g., systemic lupus erythematosus) and B-cell malignancies, making this antibody valuable for both basic research and clinical investigations.
These antibodies are typically validated for specificity using knockout cell lines or phosphorylation-blocking peptides to ensure accurate detection. Researchers utilize them to explore mechanisms of BCR signaling, immune tolerance, and therapeutic targeting of aberrant kinase activity in diseases linked to B-cell dysfunction.
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