| Code | CSB-RA156557A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| IHC | 1:50-1:200 |
SIRT5 belongs to the sirtuin family of NAD-dependent deacylases and plays a distinctive role in mitochondrial metabolism. Unlike other sirtuins that primarily remove acetyl groups, SIRT5 demonstrates robust desuccinylase and demalonylase activity, making it a critical regulator of metabolic pathways including fatty acid oxidation, the urea cycle, and ketone body production. Its mitochondrial localization positions SIRT5 as a key player in cellular energy homeostasis, with growing evidence linking its dysregulation to metabolic disorders, cardiovascular disease, and cancer progression.
This recombinant monoclonal antibody, generated from clone 9H12, offers researchers the reproducibility essential for longitudinal studies and multi-site collaborations. Because the antibody sequence is defined and produced through recombinant expression in rabbit host cells, you can expect consistent performance across lots, eliminating the variability that often complicates experiments using traditional hybridoma-derived antibodies. The antibody was raised against a synthetic peptide derived from human SIRT5, ensuring precise epitope targeting.
Validation in immunohistochemistry demonstrates reliable detection in paraffin-embedded human kidney tissue, where SIRT5 expression is particularly relevant given the kidney's high metabolic demands. Using a Leica Bond system with citrate buffer antigen retrieval and HRP-polymer detection, clear staining was achieved at 1:100 dilution, with a recommended working range of 1:50 to 1:200. The antibody is also validated for ELISA applications, providing flexibility for both tissue-based localization studies and quantitative protein analysis.
Whether investigating mitochondrial dysfunction in metabolic disease, exploring epigenetic regulation in cancer models, or examining cardiovascular pathophysiology, this SIRT5 antibody delivers the specificity and consistency your research demands.
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