MyD88 Antibody / Myeloid differentiation primary response protein 88 (R30745)

Immunohistochemistry analysis of MYD88 expression in human tonsil tissue. Paraffin-embedded human tonsil sections were subjected to heat-mediated antigen retrieval in EDTA buffer (pH 8.0) and incubated with anti-MYD88 antibody, followed by HRP-conjugated secondary antibody and DAB chromogen development. Brown immunoreactivity is observed predominantly in lymphoid cells, consistent with cytoplasmic MYD88 expression in immune cell populations, with hematoxylin nuclear counterstain (blue).

Immunohistochemistry analysis of MYD88 expression in human colon cancer tissue. Paraffin-embedded human colon cancer sections were subjected to heat-mediated antigen retrieval in EDTA buffer (pH 8.0) and incubated with anti-MYD88 antibody, followed by HRP-conjugated secondary antibody and DAB chromogen development. MYD88 staining is observed mainly in tumor-associated epithelial cells and infiltrating immune cells, consistent with cytoplasmic adaptor protein localization, with hematoxylin nuclear counterstain (blue).

Western blot analysis of MYD88 expression. Whole cell lysates from human Jurkat cells (lane 1), human HepG2 cells (lane 2), human MOLT-4 cells (lane 3), human K562 cells (lane 4), rat liver tissue (lane 5), and mouse liver tissue (lane 6) were separated by SDS-PAGE and probed with anti-MYD88 antibody. A specific immunoreactive band is detected at approximately 35 kDa across multiple samples, corresponding to MYD88. The predicted molecular weight of Myeloid differentiation primary response protein 88 is approximately 33 kDa, and the slightly higher apparent molecular weight observed on SDS-PAGE is consistent with commonly reported migration behavior for this adaptor protein.

Immunoprecipitation and western blot analysis of MYD88 expression. Human HepG2 whole cell lysates were used for immunoprecipitation with anti-MYD88 antibody. Lane 1 shows input HepG2 whole cell lysate (30 ug). Lane 2 shows immunoprecipitation performed using rabbit control IgG instead of the primary antibody, serving as a negative control. Lane 3 shows immunoprecipitation using anti-MYD88 antibody incubated with HepG2 whole cell lysate (500 ug). Immunoprecipitated proteins were resolved by SDS-PAGE, transferred to membrane, and detected using anti-MYD88 antibody followed by HRP-conjugated goat anti-rabbit IgG secondary antibody. A specific band corresponding to MYD88 is detected at approximately 35 kDa, consistent with the predicted molecular weight of Myeloid differentiation primary response protein 88. The higher molecular weight band observed around 50 kDa corresponds to the IgG heavy chain.