Tris hcl buffer

The paraffin-embedded bladder tissues were cut into 4 μm sections for immunological analysis. For immunohistochemical staining, the sections were deparaffinated, hydrated and incubated with primary F4/80 antibodies at 4 °C overnight. After washing in Tris-HCl buffer (Beyotime Biotechnology) mixed with 0.1% Tween 20 (Beyotime Biotechnology), these sections were continually incubated with a secondary antibody labeled with hydrogen peroxide oxidoreductase. All these stains were visualized with an Olympus microscope (Tokyo, Japan). For immunofluorescence staining, after the sections were incubated with the primary F4/80 antibody at 4 °C overnight and the secondary antibodies for 1 h at room temperature; appropriate second primary antibodies (CD86, with dilution 1:80/CD163, dilution 1:100) were applied at 4 °C overnight, and the second secondary antibodies were applied for another 1 h at room temperature. Then, the sections were counterstained with 4,6-diamino-2-phenylindole. Images were collected with a Zeiss Axio Scan.Z1 scanner (Carl Zeiss, Jena, Germany).

All oligonucleotides used in this work were synthesized by Sangon Biotech Co., Ltd. Detailed sequences are listed in the SI Appendix. Phosphate-buffered saline (PBS) buffer, DEPC-treated water (diethyl pyrocarbonate), and Tris-EDTA buffer were purchased from Sangon Biotech Co., Ltd. The streptavidin-functionalized MNP, Tris-(2-carboxyethyl)-phosphine hydrochloride (TCEP), and sodium dodecyl sulfate (SDS) were purchased from Aladdin. Proteinase K and Tris ⋅ HCl buffer were purchased from Beyotime Biotechnology. Aβ_1–42 peptide and monoclonal antibodies (mAbs) of Aβ_1–42 (clone 12F4) specific to the C-termini and a mAb capable of binding to the N terminus of Aβ_1–42 peptide (clone 6E10) were obtained from BioLegend, Inc. The streptavidin-functionalized AuNPs were purchased from Nanopartz. Thiol-Poly(ethylene glycol) (PEG)-hydroxyl (molecular weight: 500 Da) Thiol-PEG-biotin (molecular weight: 3,400 Da), and streptavidin were purchased from Sigma-Aldrich. All solutions were prepared with deionized water (18.2 MΩ ⋅ cm⁻¹) from a Millipore system. All experiments were repeated in triplicates unless mentioned otherwise.