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SerpinB2 binds misfolded proteins and suppresses BSA aggregation in vitro.
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posted on 2015-06-17, 03:45 authored by Jodi A. Lee, Justin J. Yerbury, Natalie Farrawell, Robert F. Shearer, Patrick Constantinescu, Danny M. Hatters, Wayne A. Schroder, Andreas Suhrbier, Mark R. Wilson, Darren N. Saunders, Marie RansonA–C. Dose dependent binding of SerpinB2 to native and misfolded proteins was determined using ELISA. Data represent mean absorbance (A490) ± SEM (n = 3); D. Real-time turbidity assay of DTT-induced BSA aggregation in the absence or presence of SerpinB2, αB-crystallin or SerpinB14 (w/w ratio). Data represent mean absorbance (A490) ± SEM (n = 3).
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paiSerpinB 2amyloid beta fibril formationupsserine protease inhibitorscompartmentalize aggregating proteinsCytoprotective Inclusion Formation SerpinB 2display cytoprotective propertiesmefSerpinB 2 expressionBinding Misfolded ProteinsInclusion body formationcell viabilityclade B familyGFP reporter systemurokinase plasminogen activator
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