| Code | CSB-RA151186A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
| FC | 1:50-1:200 |
Heat shock protein 70 (HSP70), encoded by the highly homologous HSPA1A and HSPA1B genes, serves as a critical molecular chaperone that protects cells from proteotoxic stress. This inducible member of the HSP70 family plays essential roles in protein folding, prevention of aggregation, and cellular stress responses, making it a key target in studies of cancer biology, neurodegeneration, and cellular stress pathways. Elevated HSP70 expression is frequently observed in tumor cells, where it contributes to survival mechanisms and therapeutic resistance.
This recombinant rabbit monoclonal antibody (clone 9C11) offers the reproducibility and consistency that demanding research applications require. Generated against a synthetic peptide derived from human HSPA1A/HSPA1B and produced using recombinant technology, this antibody provides sequence-defined specificity with minimal lot-to-lot variation, ensuring reliable results across extended studies and collaborative projects.
Validation across multiple platforms demonstrates the versatility of this antibody for diverse experimental workflows. Western blot analysis confirms detection of the expected 70 kDa band in human HEK293 and U937 cell lysates, as well as mouse NIH/3T3 lysates, supporting cross-species reactivity between human and mouse samples. Immunohistochemistry staining in human testis tissue reveals clear target localization, while flow cytometry analysis in HeLa cells shows distinct positive signal separation from isotype controls, enabling quantitative assessment of HSP70 expression at the single-cell level.
Whether investigating stress response mechanisms, characterizing tumor cell survival pathways, or exploring chaperone function in disease models, this affinity-purified antibody delivers the specificity and cross-species reactivity needed to advance your research across multiple experimental approaches.
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