Figure 4
Figure 4. TLT-1 is enriched in HA+ samples in resting and activated platelets. (A) Domain organization of full-length TLT-1 and the TLT-1 splice variant depicting an Ig-like V-type domain (blue) with 4 cysteine residues followed by a single-pass transmembrane (TM) domain (green). The TLT-1 splice variant has a truncated cytoplasmic tail and does not contain the 3 intracellular cysteines or ITIM region.32 (B) Western blot analysis of TLT-1 using ABE-purified palmitoylated proteins from resting and thrombin-activated platelets. Arrow indicates full-length TLT-1; and arrowhead, a 25 kDa TLT-1 splice variant. Bands seen directly below full-length TLT-1 and bands seen below the TLT-1 splice variant are degradation products.33 Also shown are 20 μg of the sample inputs that represent the protein sample added to the streptavidin agarose beads.

TLT-1 is enriched in HA+ samples in resting and activated platelets. (A) Domain organization of full-length TLT-1 and the TLT-1 splice variant depicting an Ig-like V-type domain (blue) with 4 cysteine residues followed by a single-pass transmembrane (TM) domain (green). The TLT-1 splice variant has a truncated cytoplasmic tail and does not contain the 3 intracellular cysteines or ITIM region.32  (B) Western blot analysis of TLT-1 using ABE-purified palmitoylated proteins from resting and thrombin-activated platelets. Arrow indicates full-length TLT-1; and arrowhead, a 25 kDa TLT-1 splice variant. Bands seen directly below full-length TLT-1 and bands seen below the TLT-1 splice variant are degradation products.33  Also shown are 20 μg of the sample inputs that represent the protein sample added to the streptavidin agarose beads.

Close Modal

or Create an Account

Close Modal
Close Modal