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Reveal protein profiles
The smallest changes upstream influence results downstream.
Defining the role of proteins as drugs, drug targets or disease biomarkers is crucial to the development of new therapeutics and our understanding of disease mechanisms. Yet changes to protein - and peptide profiles begin within seconds of a tissue being sampled. Vital information about the original protein profile may be destroyed or distorted, leading to inter-sample variation, risk of incorrect data interpretation and potentially misleading conclusions.
Conventional approaches to inhibiting these changes, such as using inhibitor cocktails, pH changes or cross-linking, may be reversible, involve the use of toxic compounds and interfere with downstream analytical techniques.
Rapid heat stabilization preserves protein profiles by instantly and permanently denaturing the proteolytic enzymes responsible for rapid biological changes.
Using the Stabilizor system to heat-stabilize tissue samples:
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Prevents ex vivo degradation products from compromising downstream analysis
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Avoid use of additives that may interfere with analytical techniques
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Increases analytical reproducibility by minimizing inter-sample variation
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Facilitates confident data interpretation
Inhibition of protease activity
Heat-stabilized samples show a significant lower level of protease activity compared to snap-frozen samples. Activity measured using fluorescent protease kit (Pierce).
Heat stabilization reduced protein fragmentation
Artefacts from protein degradation generated post-mortem or during sample preparation should be prevented by preserving the native proteome at the moment of sampling.
When compared with conventional snap-freezing, heat stabilization of brain tissue was found to have beneficial effects on protein stabilization during sample preparation. High molecular weight proteins were preserved and protein fragmentation reduced. Assessing the use of thermal treatment to preserve the intact proteomes of post-mortem heart and brain tissue, AA. Robinson et al. UCD Conway, Ireland, Proteomics. 2009 Oct;9(19):4433-44).
