| 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 | 1/100-1/200 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | ALK; ALK tyrosine kinase receptor; Anaplastic lymphoma kinase; CD antigen CD246 |
| Entrez GeneID | 238 |
| WB Predicted band size | Calculated MW: 176 kDa; Observed MW: 176 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 |
| Immunogen | Synthetic peptide of human ALK |
| 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Phospho-ALK (Tyr1604)抗体的虚构参考文献示例(注：实际文献需通过数据库检索验证)：
1. **文献名称**：*Phosphorylation of ALK at Tyr1604 Mediates Resistance to Targeted Therapy in Neuroblastoma*
**作者**：Chen L, et al.
**摘要**：研究揭示了ALK酪氨酸1604位点(Tyr1604)磷酸化在神经母细胞瘤中对ALK抑制剂(如克唑替尼)耐药性的作用，通过Phospho-ALK (Tyr1604)抗体证实该位点磷酸化导致下游STAT3信号异常激活。
2. **文献名称**：*ALK Tyrosine 1604 Phosphorylation Promotes Tumor Growth in Non-Small Cell Lung Cancer*
**作者**：Wang Y, et al.
**摘要**：利用Phospho-ALK (Tyr1604)特异性抗体，研究发现Tyr1604磷酸化在非小细胞肺癌(NSCLC)中与ALK融合蛋白(如EML4-ALK)的持续激活相关，促进肿瘤增殖和转移。
3. **文献名称**：*Development and Validation of a Phospho-ALK (Tyr1604) Antibody for Immunohistochemical Analysis*
**作者**：Smith R, et al.
**摘要**：本文描述了一种新型Phospho-ALK (Tyr1604)抗体的开发与验证，证明其在福尔马林固定石蜡包埋组织中的特异性，可用于临床样本中ALK活化状态的评估。
4. **文献名称**：*Structural Basis of ALK Activation by Tyr1604 Phosphorylation in Inflammatory Myofibroblastic Tumors*
**作者**：Garcia M, et al.
**摘要**：通过结构生物学和Phospho-ALK (Tyr1604)抗体的应用，阐明Tyr1604磷酸化诱导ALK二聚化及激酶活性增强的分子机制，为炎性肌纤维母细胞瘤的治疗提供新靶点。
**建议**：实际研究中可通过PubMed或Google Scholar以关键词“Phospho-ALK Tyr1604”或“ALK phosphorylation site 1604”检索最新文献，并关注高影响力期刊(如*Nature Cancer*、*Clinical Cancer Research*)。
Phospho-ALK (Tyr1604) antibody is a specialized tool used to detect the activated form of the Anaplastic Lymphoma Kinase (ALK), a receptor tyrosine kinase involved in cell growth and survival signaling. ALK gains oncogenic potential through genetic alterations like chromosomal translocations (e.g., NPM-ALK in anaplastic large cell lymphoma) or activating mutations, which drive constitutive phosphorylation and downstream signaling via pathways such as MAPK/ERK, PI3K/AKT, and JAK/STAT. The phosphorylation of tyrosine 1604 (Y1604) in the kinase domain is critical for ALK activation, as it stabilizes the active conformation required for substrate binding and signaling.
This antibody specifically recognizes ALK when phosphorylated at Y1604. making it valuable for research on ALK-driven cancers, including neuroblastoma, non-small cell lung cancer (NSCLC), and lymphomas. It is widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence to assess ALK activation status, monitor therapeutic responses to ALK inhibitors (e.g., crizotinib, alectinib), and study resistance mechanisms. Dysregulated ALK signaling is a key therapeutic target, and phospho-specific antibodies help elucidate its role in tumor progression and drug sensitivity. Proper validation using ALK-mutated or inhibitor-treated samples is essential to ensure specificity, as cross-reactivity with other phosphorylated tyrosine residues can occur.
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