Key result
Polyclonal antibodies detect a single obscurin isoform in long-tailed ground squirrel striated muscle without seasonal changes.
Polyclonal antibodies identified a 115 kDa low molecular weight isoform of obscurin in the striated muscles of long-tailed ground squirrels, with no seasonal variation.
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Antibodies enable obscurin isoform detection in hibernator muscle; leaves open functional roles in seasonal cardiac adaptation.
The obtained polyclonal antibodies specific to the N-sequence (76–289 aa) of obscurin of the long-tailed ground squirrel () were used to study the isoform composition of this protein in two striated muscles: the myocardium of the left ventricle and M. gastrocnemius medialis. One low molecular weight isoform of obscurin with a molecular weight of 115 kDa has been identified. No other isoforms of obscurin, including giant A- and B-isoforms, have been detected. Seasonal changes in the levels of the low molecular weight obscurin isoform visualized in the cardiac and skeletal muscles of long-tailed ground squirrels were not observed. Further research could focus on sequencing the obscu gene of long-tailed ground squirrels and analyzing obscurin transcripts to obtain antibodies specific to the giant isoforms of this protein.
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T.A. Uryupina (2025) studied this question. Polyclonal antibodies detected a single 115 kDa obscurin isoform in long-tailed ground squirrel heart and muscle, with no seasonal changes observed.
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