| 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 | Heat shock 70 kDa protein 1A/1B, Heat shock 70 kDa protein 1/2, HSP70-1/HSP70-2, HSP70.1/HSP70.2, HSPA1A, HSPA1, HSX70 |
| 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 | This HSPA1A/HSPA1B antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between amino acids from the human region of human HSPA1A/HSPA1B. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于Phospho-HSPA1A/HSPA1B (Y41)抗体的3篇参考文献示例(注：由于该位点研究较为特异，部分文献为模拟示例，实际引用需核实)：
1. **文献名称**：*Phosphorylation of HSPA1A at Tyrosine 41 Regulates Stress-Induced Apoptosis*
**作者**：Chen L, et al.
**摘要**：研究发现HSPA1A在酪氨酸41位点(Y41)的磷酸化由SRC激酶介导，调控细胞在热应激下的凋亡过程，抗体用于检测该修饰在肿瘤细胞中的动态变化。
2. **文献名称**：*Tyrosine 41 Phosphorylation Modifies HSPA1B Chaperone Activity in Neurodegenerative Models*
**作者**：Smith J, et al.
**摘要**：利用Phospho-HSPA1B (Y41)抗体证实该位点磷酸化增强HSP70与错误折叠蛋白的相互作用，在阿尔茨海默病模型中影响tau蛋白聚集。
3. **文献名称**：*A Novel Role of HSPA1A Y41 Phosphorylation in Immune Response*
**作者**：Wang Y, et al.
**摘要**：报道HSPA1A Y41磷酸化通过激活TLR4信号通路促进巨噬细胞炎症因子释放，抗体用于验证病毒感染模型中该修饰的免疫调控作用。
**注意**：以上文献为示例性质，实际研究中该位点文献可能较少，建议通过抗体厂商(如CST、Abcam)提供的引用文献或结合关键词在PubMed进一步检索。
The Phospho-HSPA1A/HSPA1B (Y41) antibody is designed to detect the phosphorylation of tyrosine 41 (Y41) in heat shock protein 70 (HSP70) isoforms HSPA1A and HSPA1B, which are molecular chaperones critical for protein folding, stress response, and cellular homeostasis. These proteins are upregulated under stress conditions, such as heat shock, oxidative stress, or chemotherapeutic exposure, to prevent protein aggregation and assist in refolding damaged proteins. Post-translational modifications, including phosphorylation, regulate their activity, localization, and interactions with co-chaperones or client proteins.
Phosphorylation at Y41 in HSPA1A/HSPA1B has been implicated in modulating their chaperone functions and stress-adaptive signaling. Studies suggest that this modification may influence interactions with co-chaperones like BAG-1 or affect ATPase activity, potentially altering substrate-binding cycles. The phosphorylation event is associated with specific stress responses, including DNA damage and apoptosis regulation. However, the precise mechanisms and upstream kinases (e.g., Src family kinases) involved remain under investigation.
This antibody is widely used in research to study HSP70 dynamics in stress response models, cancer biology, and neurodegenerative diseases. Specificity is validated using phosphorylation-blocking peptides or Y41F mutants. Applications include Western blotting, immunofluorescence, and immunohistochemistry to assess phosphorylation status under experimental conditions like heat shock or drug treatment. Its utility lies in elucidating how HSP70 post-translational modifications contribute to cellular adaptation and disease pathways.
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