Article thumbnail

SerpinB2 binds misfolded proteins and suppresses BSA aggregation <i>in vitro</i>.

By Jodi A. Lee (756105), Justin J. Yerbury (756106), Natalie Farrawell (756107), Robert F. Shearer (294519), Patrick Constantinescu (756108), Danny M. Hatters (306988), Wayne A. Schroder (54052), Andreas Suhrbier (130162), Mark R. Wilson (278126), Darren N. Saunders (294516) and Marie Ranson (25441)

Abstract

<p><b>A–C.</b> Dose dependent binding of SerpinB2 to native and misfolded proteins was determined using ELISA. Data represent mean absorbance (A<sub>490</sub>) ± SEM (n = 3); <b>D.</b> 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 (A<sub>490</sub>) ± SEM (n = 3).</p

Topics: Biological Sciences, pai, SerpinB 2, amyloid beta fibril formation, ups, serine protease inhibitors, compartmentalize aggregating proteins, Cytoprotective Inclusion Formation SerpinB 2, display cytoprotective properties, mef, SerpinB 2 expression, Binding Misfolded Proteins, Inclusion body formation, cell viability, clade B family, GFP reporter system, urokinase plasminogen activator
Year: 2015
DOI identifier: 10.1371/journal.pone.0130136.g004
OAI identifier: oai:figshare.com:article/1452051
Provided by: FigShare
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • https://figshare.com/articles/... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.