| Code | CSB-RA010242A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IHC | 1:50-1:200 |
| IP | 1:200-1:1000 |
HDAC6 is a unique class IIb histone deacetylase that plays a central role in cytoplasmic protein quality control, aggresome formation, and stress response pathways. Unlike nuclear HDACs, HDAC6 primarily deacetylates cytoplasmic substrates including α-tubulin, HSP90, and cortactin, making it a compelling target for researchers investigating cellular stress responses, autophagy, and neurodegenerative disease mechanisms. Its involvement in cancer cell migration and metastasis has also positioned HDAC6 as an emerging therapeutic target in oncology research.
This recombinant monoclonal antibody, generated from clone 2H12 in rabbit, offers the reproducibility and sequence-defined consistency that demanding experimental workflows require. Because recombinant production eliminates the batch variability inherent in traditional hybridoma methods, researchers can confidently compare results across extended studies without concerns about antibody drift between lots.
Validation testing demonstrates robust performance across multiple applications. Western blot analysis detects HDAC6 in a range of human cell lines including HeLa, MCF-7, HepG2, K562, and Jurkat lysates, with an observed band at approximately 160 kDa. This migration above the predicted molecular weights of 132 and 115 kDa likely reflects post-translational modifications such as phosphorylation or ubiquitination, which are well-documented for this protein. Immunohistochemistry staining has been validated in paraffin-embedded human liver cancer tissue, while immunoprecipitation successfully enriches HDAC6 from HepG2 lysates, enabling downstream interaction studies or activity assays.
For researchers exploring epigenetic regulation, nuclear signaling, or the expanding landscape of HDAC6 biology in disease contexts, this antibody provides a reliable tool with demonstrated versatility across biochemical and tissue-based applications.
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