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Independent Antibody Validation in Cell lines (Figure 2) shows similar MYD88 expression profile in both human and mouse cell lines detected by two independent anti-MYD88 antibodies that recognize different epitopes, 2125 against internal domain and 2127 against the C-terminus domain. MYD88 proteins are detected in all the tested cell lines at different expression levels by the two independent antibodies. Additionally, Figure 2 shows the mouse MYD88 protein in NIH/3T3 cells migrates slightly faster than human isoform 1 detected by both MYD88 antibodies (2125 and 2127), which is well correlated with their calculated molecular masses (33.8 kDa vs 35.4 kDa).
Independent Antibody Validation in Human Tissues (Figure 3) shows similar MYD88 expression profile in human tissues detected by two independent anti-MYD88 antibodies (2125 and 2127). MYD88 proteins are detected by the two independent antibodies in liver, kidney, lung, thymus, colon, bladder and breast of human tissues at different expression levels, but not in heart, brain, skin and pancreas.
Animal Species Reactivity (Figure 4): Anti-MYD88 antibodies (2125 and 2127) can detect the expression of MYD88 protein in the liver and spleen of all tissues and mouse heart, but not in human heart. Additionally, Figure 4 also shows MYD88 protein detected by both MYD88 antibodies (2125 and 2127) in human liver and Daudi cells migrates slightly slower than that in the tissues of mouse and rat, which is well correlated with their calculated molecular masses (35.4 kDa vs 33.8 kDa and 33.9kD).
siRNA knockdown validation (Figure 5): Anti-MYD88 antibody (2125) specificity was further verified by MYD88 specific siRNA knockdown. MYD88 signal in HeLa cells transfected with MYD88 siRNAs was weaker in comparison with that in HeLa cells transfected with control siRNAs.
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A431 Lysate
MyD88 Peptide
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