aβ42 fitc peptide  (Macklin Inc)

Journal: Translational Psychiatry

Article Title: Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice

doi: 10.1038/s41398-026-04002-9

Figure Lengend Snippet: ( A - C ) Aβ40 and Aβ42 levels in the soluble TBS fractions ( A ), detergent soluble (TBS-X) fractions ( B ), and insoluble neutralized formic acid (FA) fractions ( C ) of cortical brain homogenates in the 5xFAD mice were measured by ELISA at 8 months of age, normalized to protein concentrations of each fraction. ( D ) Soluble oligomeric Aβ (oAβ) levels in the TBS-X fractions of cortical brain homogenates in the 5xFAD mice were measured by ELISA at 8 months of age, normalized to protein concentrations. ( E, F ) Amounts of full-length APP in the TBS-X fractions of mouse cortical lysates were measured by western blot at 8 months of age, normalized to those of β-actin (ACTB). Data are expressed as means ± SEM (GFP: N = 12; APOE3: N = 18; APOE3Ch: N = 13; Open circles: females, closed circles: males). Injection group differences were analyzed using two-way ANOVA, with Tukey’s multiple comparisons test, adjusting for sex. *, P < 0.05; **, P < 0.01.

Article Snippet: Recombinant Aβ42 monomer (1 mg/ml) (Stressmarq, #SPR-485) was incubated at room temperature for 10 min. To dissolve the peptide, 7.5 μl of cold DMSO (Sigma Aldrich) was added, followed by 92.5 μl of cold PBS (PH 7.4) to reach a final concentration of 220 μM monomeric Aβ42.

Techniques: Enzyme-linked Immunosorbent Assay, Western Blot, Injection

Journal: Translational Psychiatry

Article Title: Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice

doi: 10.1038/s41398-026-04002-9

Figure Lengend Snippet: ( A ) Isogenic iPSC-derived astrocytes (iPSC-ACs) with homozygous APOE3 (left) and APOE3Ch (right) were immunostained for GFAP (green) and S100b (red). DAPI (blue) stains nuclei. Scale bars: 100 µm. ( B ) APOE mRNA levels in the iPSC-ACs were measured by RT-qPCR, normalized to those of β-actin ( ACTB ). ( C, D ) Amounts of APOE in the conditioned medium (CM) from iPSC-ACs were measured by western blot, normalized to protein amounts of cell lysates. ( E ) Effects of the CM from iPSC-ACs on Aβ42 aggregation was assessed by western blot using 6E10 antibody. ( F - G ) Populations of Aβ fibrils (F; > 150 kDa), oligomers (G; 37–150 kDa), and monomers ( H ; < 10 kDa) were quantified. Data expressed as means ± SEM (n = 3–5 independent differentiation batches). Group differences were analyzed using two-tailed student t-test or one-way ANOVA with Tukey’s multiple comparisons test. *, P < 0.05.

Article Snippet: Recombinant Aβ42 monomer (1 mg/ml) (Stressmarq, #SPR-485) was incubated at room temperature for 10 min. To dissolve the peptide, 7.5 μl of cold DMSO (Sigma Aldrich) was added, followed by 92.5 μl of cold PBS (PH 7.4) to reach a final concentration of 220 μM monomeric Aβ42.

Techniques: Derivative Assay, Quantitative RT-PCR, Western Blot, Two Tailed Test

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Effect of bFg and hFg on the amyloid fibril formation of Aβ42. (A) Time courses of ThT fluorescence intensities with bFg (left) or hFg (right). Error bars represent one standard deviation ( n = 3). The lines indicate curves obtained by fitting using . (B) AFM image of an oligomer taken 1 h after incubation without bFg or hFg. Scale bar: 500 nm. (C) AFM image of amyloid fibrils taken 7 h after incubation without bFg or hFg. Scale bar: 500 nm. (D) The midpoint of the sigmoidal increase (τ half ) and the fluorescence intensity at the plateau phase ( I plat ) obtained from curve fitting of the data in panel A using . Error bars represent values obtained from curve fitting. The value for the control (without bFg or hFg) is indicated by black lines.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques: Fluorescence, Standard Deviation, Incubation, Control

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Dot blot results in the presence of bFg (A) or hFg (B), respectively. Samples were taken at 1 h after the start of amyloid fibril formation. Sample names are numbered and listed at the bottom of each panel. The intensities are normalized using that of Aβ42 only (sample ①). The error bars indicate one sigma values ( n = 3 ∼ 15). Examples of blots are shown below the bars.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques: Dot Blot

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: AUC profiles of Aβ42 in the presence of (A) bFg or (B) hFg at 1 h during amyloid fibril formation. Each panel displays an overview of the profiles (top) and magnified views along each axis (bottom). Each profile is shifted along the y -axis for clarity. Peaks marked with asterisks represent minor small components present in bFg or hFg.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques:

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Effect of bFg and hFg on Aβ42 oligomer formation, as observed in AFM images taken 1 h after the start of amyloid fibril formation. (A) Aβ42 only. (B) With 3 μM bFg. (C) With 3 μM hFg. Scale bars indicate 500 nm.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques:

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Cell viability in the presence of Aβ42 with or without bFg or hFg. Error bars represent ± 2 SD ( n = 3). P-values were obtained by a one-sided two-sample t test assuming equal variances.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques:

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Proposed binding manners between Aβ42 and the fibrinogen molecules, and resultant effects on the inhibition of the Aβ42 amyloid fibril formation and cell toxicity. K d app values were obtained using eq S6 . The representations of the colors of bFg or hFg molecules are as follows: The N-terminal region of Aα chain, red; the C-terminal region of Aα chain, i.e., αC region, orange; the Bβ chain, blue; the γ chain, green. Globular domains are represented by ellipses. See details in the main text.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques: Binding Assay, Inhibition