| Code | CSB-RA055227A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| IHC | 1:50-1:200 |
Cathepsin H is a lysosomal cysteine proteinase belonging to the papain superfamily that plays essential roles in protein degradation and processing within the endosomal-lysosomal system. This enzyme exhibits both endopeptidase and aminopeptidase activities, enabling it to participate in diverse cellular processes including antigen processing, neuropeptide maturation, and extracellular matrix remodeling. In neuroscience research, cathepsin H has garnered significant attention for its involvement in neuronal protein homeostasis and its potential contributions to neurodegenerative pathways.
This recombinant monoclonal antibody targeting human CTSH offers researchers the reproducibility advantages inherent to recombinant technology. Because the antibody sequence is defined and production occurs in controlled expression systems, you can expect consistent performance across different lots, eliminating the variability that can complicate long-term studies or multi-site collaborations. The rabbit IgG format, generated against a synthesized peptide from human CTSH, provides reliable specificity for your target.
Validation through immunohistochemistry demonstrates this antibody's utility for examining cathepsin H expression in tissue contexts. Testing in paraffin-embedded human lung tissue and human breast cancer tissue at 1:100 dilution using citrate buffer antigen retrieval confirms its compatibility with standard FFPE workflows on automated platforms such as the Leica Bond system. The recommended working range of 1:50 to 1:200 for IHC applications provides flexibility for optimization across different tissue types and fixation conditions.
Whether you are investigating cathepsin H expression patterns in normal physiology, exploring its dysregulation in cancer biology, or examining its role in neurological processes, this antibody provides a dependable tool for immunohistochemical analysis of human specimens.
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