Amyloid Beta Antibody APP/3345 / Beta Amyloid Antibody [clone APP/3345] (V8733)

Amyloid Beta Antibody APP/3345 in U-87 MG Cells IF. Immunofluorescence staining of PFA-fixed human U-87 MG cells with Amyloid Beta Antibody clone APP/3345 shows green cytoplasmic staining with a granular to punctate distribution and areas of increased perinuclear signal. Red nuclear counterstaining delineates the nuclei, which show little green fluorescence. The observed cellular distribution demonstrates recognition by the Beta Amyloid Antibody in fixed U-87 MG cells.

Amyloid Beta Antibody APP/3345 in Human Brain Tissue IHC. Immunohistochemistry staining of FFPE human brain tissue with Amyloid Beta Antibody clone APP/3345 demonstrates widespread brown staining throughout the neuropil with more prominent staining associated with scattered cells and cellular processes. Tissue sections underwent HIER in 10 mM Tris with 1 mM EDTA, pH 9, for 20 min followed by cooling before testing. The Beta Amyloid Antibody produces a distinct tissue-associated staining pattern against the hematoxylin-counterstained brain section.

Amyloid Beta Antibody APP/3345 Protein Microarray Validation. Protein Microarray Validated analysis of Amyloid Beta Antibody clone APP/3345 on a HuProt microarray containing more than 19,000 full-length human proteins identifies the intended amyloid beta/APP target as the highest-ranked signal, with substantial separation from the next-ranked proteins. The Z-score represents signal strength in standard deviations above the array mean, while the S-score measures the difference between the target Z-score and the next-highest signal. The pronounced separation of the intended target supports the specificity of this Beta Amyloid Antibody in the protein microarray assay.

Purified Amyloid Beta Antibody APP/3345 Reducing and Non-Reducing SDS-PAGE. SDS-PAGE analysis of purified, BSA-free Amyloid Beta Antibody clone APP/3345 shows prominent antibody heavy and light chains at approximately 50 and 25 kDa under reducing conditions. Under non-reducing conditions, the predominant intact antibody species migrates at approximately 150 kDa, with little additional protein staining visible. The gel demonstrates the expected molecular composition and integrity of the purified Beta Amyloid Antibody preparation.