Protein samples
can be challenging to analyze due to the presence of high-abundance proteins
masking lowabundance proteins of interest, such as biomarkers and
novel physiological mediators. Cyclophilins
are chaperones involved in the cis/trans isomerization of peptidyl-prolyl bonds
in peptides or proteins and have been found in every organism sequenced to
date.
Although
considerable progress has been made in the characterization of some
cyclophilins expressed in diverse parasites invading humans, the main aspects
of low-abundance members of this family remain unknown.
In the present
work, we present that the combined strategy of using more specific antibodies
and increasing the presence of subcellular proteins in the sample, allowed us
to confirm the expression of a 21.1 kDa cyclophilin for the first time in
Trypanosoma cruzi.
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