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Both isoforms were tissue-enriched in the mice brain and testis, and displayed different intra-nuclear locations, possibly controlled by the third RS-domain [ 30].
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Both isoforms were expressed in all tissues, with an overall higher expression level of UGPase1 relative to UGPase2.
Both isoforms were mainly extracted with PBS.
Both isoforms are present in normal tissues, the expression of which is tissue-specific, with the full version being more abundant in most tissues [ 1].
Both isoforms are thought to function in various tissues in a mostly redundant manner.
PPARγ1 is ubiquitously expressed and PPARγ2 is strictly expressed in adipose tissues, while both isoforms are strongly induced during adipocyte differentiation.
Both isoforms are co-expressed in most CEACAM1-expressing tissues, and the ratio between the two isoforms determines the signalling outcome [ 8- 12].
Systematic analysis by RT-PCR proved that both isoforms are expressed in all 29 NE and 8 normal tissue samples investigated, with the constant prevalence of the CAG- isoform, as also confirmed by human EST database analysis.
Both isoforms are quite broadly expressed on mRNA level in many human tissues.
We annotated AS events as modified protein when both isoforms are protein-coding, loss-of-function if only the reference isoform is protein-coding, gain-of-function if only the alternative isoform is protein-coding, and non-coding if both isoforms are non-coding.
Both isoforms are biochemically active.
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