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The major isoforms are CEACAM1-4L and CEACAM1-4S that possess an extracellular aminoterminal IgV-like domain (N), followed by three IgC2-like domains (A1, B, A2) and a transmembrane domain.

The major isoforms are determined by alternative mRNA splicing of exon 10 generating tau with three (3R) or four (4R) ∼32 amino acid imperfect repeats in the microtubule binding domain.

The most commonly expressed or major isoforms are PlGF-1 (131 amino acids) and PlGF-2 (152 amino acids) [ 27].

Multiple isoforms of P63 exist in zebrafish (as in other organisms); the major isoforms are known as ΔNP63 and TAP63.

The two major isoforms are RPGR1 19 (exons 1 19) and RPGRORF15 (exons 1 15 + a part of intron 15 ORF15).

The major isoforms are the most conserved, and there is not a single non-synonymous substitution among the Drosophila β1 and α1 tubulins.

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Consistent with our earlier fractionation and immunohistochemical studies on dysbindin-1 in mouse and human brain tissue [43], all three of its major isoforms were concentrated in synaptic tissue though high concentrations of isoform B were also found in cell nuclei (Figure 4A).

Confirmation of the sequence for the Leishmania major isoforms was obtained from Matt Rogers (Sanger institute).

Alternative splicing generates several APP mRNAs with the three major isoforms being APP695, APP751, and APP770 [ 141].

The major isoforms were 32-34 nts long (for tRF5-ValGTG) and 30-32 nts long (for tRF5-GlyGGY).

The purified and re-chromatographed major isoform was deglycosylated to remove covalently bound carbohydrates.

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