Quantification of Stress in Space

Astronauts face various physiological and biological challenges after their descent into the cosmos including space motion sickness, bone demineralization, fatigue, and even isolation. Space physiology studies are limited due to minimal access to astronauts. Today’s technology, however, has allowed us to extract information even from small sample sizes. Blood biomarkers, anti-inflammatory cytokines, and more are easily measured and studied using ELISA kits, available through Enzo Life Sciences.

In a recent study, researchers evaluated the pro/anti-inflammatory state of two crewmembers spending six months in space. C-proteasome quantification was conducted on the astronauts, both of same sex and similar age using our Proteasome 20S α1, 2, 3, 5, 6 & 7 subunits mAb (MCP231). Proteasomes degrade unnecessary proteins by breaking peptide bonds via proteases. By quantifying these protein complexes, researchers are able to evaluate overall health, or lack thereof. At the end of the study, c-proteasome amounts were significantly higher in both subjects, indicating disease activity and an autoimmune response. Such results are consistent with the prolonged stress of spaceflight, and the inflammation that follows. Sound too sci-fi to be true? It’s not! Increased c-proteasome indicated a tissue injury, which can be compared to levels present in patients of autoimmune diseases, indicating muscle wasting.

Enzo Life Sciences provides a range of products for all your Immunology and Metabolism research needs. Our platform provides a wide range of assay kits, small molecules, antibodies, and proteins. We offer activating enzymes (E1s), conjugating enzymes (E2s), ligases (E3s) and deconjugating enzymes (DCEs), plus an innovative range of ubiquitin-, SUMO-, NEDD8-, ISG15- and FAT10-associated proteins and derivatives. Discover ubiquitin- and Ubl-reactive antibodies, kits for the study of ubiquitin, SUMO, and NEDD8 conjugation, and our easy-to-use UBIQAPTURE-Q® and SUMO-QAPTURE-T® kits for the detection and isolation of ubiquitinated and SUMOylated proteins.

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