Figure 2
Figure 2. Multimeric analysis of expressed VWF. VWF in the conditioned medium of transiently transfected HEK293T cells was analyzed by electrophoresis in 2% SDS-agarose gels and immunoblotted as described in “Multimer analysis.” Panels A and B represent 2 individual gels. In panel B, lanes were removed for clarity as shown by the separation. (A) Multimeric structure of WT-VWF (lane 1), M740I-VWF (lane 2), M740I/C1190S-VWF (lane 3), and C1190S-VWF (lane 4). (B) Multimeric composition of WT-VWF (lane 1); cysteine mutations C1272S-VWF, C1272Y-VWF, and C1099P-VWF (lanes 2-5); I1568N-VWF (lane 6); G1579R-VWF (lane 7); and G1631D-VWF (lane 8). VWF variants involving mutation of cysteines results in abnormal multimer structure.

Multimeric analysis of expressed VWF. VWF in the conditioned medium of transiently transfected HEK293T cells was analyzed by electrophoresis in 2% SDS-agarose gels and immunoblotted as described in “Multimer analysis.” Panels A and B represent 2 individual gels. In panel B, lanes were removed for clarity as shown by the separation. (A) Multimeric structure of WT-VWF (lane 1), M740I-VWF (lane 2), M740I/C1190S-VWF (lane 3), and C1190S-VWF (lane 4). (B) Multimeric composition of WT-VWF (lane 1); cysteine mutations C1272S-VWF, C1272Y-VWF, and C1099P-VWF (lanes 2-5); I1568N-VWF (lane 6); G1579R-VWF (lane 7); and G1631D-VWF (lane 8). VWF variants involving mutation of cysteines results in abnormal multimer structure.

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