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Ab40693

Manufactured by Abcam
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Ab40693 is a monoclonal antibody that targets the amyloid-beta (Aβ) peptide. It is designed for use in research applications to detect and quantify Aβ levels in various biological samples.

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Lab products found in correlation

Ab56574, by Abcam (2 mentions) Jem 1011, by JEOL (2 mentions) Ab4074, by Abcam (1 mentions) Ab86135, by Abcam (1 mentions) Hoechst 33342, by Merck Group (1 mentions) Rnase v1, by Thermo Fisher Scientific (1 mentions) Rnase a, by Thermo Fisher Scientific (1 mentions) Staurosporine, by Merck Group (1 mentions)

4 protocols using ab40693

1

Arsenite and Arsenic (V) Oxide Cytotoxicity Assay

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Sodium (meta)arsenite (NaAsO2) and sodium arsenic (V) oxide (As2O5 were purchased from Sigma-Aldrich (S7400 and 483257, respectively). For arsenite (As[III]) use, a 1 M stock solution was prepared in water and stored at RT. For arsenic (V) oxide (As[V]) use, a 218 mM stock solution was prepared in water and stored at RT. Staurosporine was purchased from Sigma (S5921), dissolved in DMSO and stored at –20°C as a 1 mM stock solution. RNAse A was purchased from Thermo Scientific™ (EN0531). RNAse V1 was purchased from Thermo Scientific™ (AM2275) and stored at –20°C in storage buffer (10 mM Tris Succinate, pH 7.5, 0.2 M KCl and 50% glycerol, v/v). The following antibodies were used: anti-TIA-1 (Abcam, ab40693, rabbit, 1:500), anti-G3BP1 (Abcam, ab56574, mouse, 1:1000), anti-cleaved Caspase-3 (Asp175) (Cell Signaling, 5A1E, rabbit, 1:500), anti-γ-H2AX(p-S139) (Upstate BioTech JBW301, mouse, 1:1000). Of note, ab40693 has been discontinued by Abcam after internal validation on TIA-1 knock-out cells (contact Abcam for further information).
Sanadgol N., König L., Drino A., Jovic M, & Schaefer M.R. (2022). Experimental paradigms revisited: oxidative stress-induced tRNA fragmentation does not correlate with stress granule formation but is associated with delayed cell death. Nucleic Acids Research, 50(12), 6919-6937.
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2

Immunostaining of Stress Granule Proteins

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Cells were grown on coverslips, washed with PBS and fixed for 20 min in 4% PFA. Cells were then permeabilized in 0.5% Triton X-100 for 3 min. After blocking, cells were immunostained for 1 h with a primary antibody, and after subsequent washes the cells were incubated for 1 h with fluorescently labeled secondary antibodies. Primary antibodies: goat anti-TIA-1 (Abcam, ab40693; 1:200), rabbit anti-eIF4B (Abcam, ab68474; 1:200), mouse anti-G3BP1 (Abcam, ab56574; 1:200), rabbit anti-G3BP2 (Abcam, ab86135; 1:1000), rabbit anti-α-tubulin (Abcam, ab4074; 1:400). Secondary antibodies: Alexa Fluor 488-labeled goat anti-mouse IgG and anti-rabbit IgG, Alexa Fluor 594-labeled goat anti-mouse IgG and anti-rabbit IgG (all from Abcam; 1:1000) and Alexa Fluor 647-labeled donkey anti-rabbit IgG (Life Technology; 1:1200). Nuclei were counterstained with Hoechst 33342 (Sigma), and coverslips were mounted in mounting medium (made in house).
Schwed-Gross A., Hamiel H., Faber G.P., Angel M., Ben-Yishay R., Benichou J.I., Ishay-Ronen D, & Shav-Tal Y. (2022). Glucocorticoids enhance chemotherapy-driven stress granule assembly and impair granule dynamics, leading to cell death. Journal of Cell Science, 135(14), jcs259629.
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3

Immunogold Labeling of Tau Aggregates

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Mixtures of tau aggregates were prepared using the ThioT aggregation assay described above. 48 h reaction mixtures with or without TIA1 were adsorbed for 2 min onto formvar/carbon-coated Nickel mesh grids, washed 2x with distilled water (dH20), treated with 2% uranyl acetate, washed 4x with dH20 and imaged at 80 kV using a JEOL JEM 1011 with a digital camera (Gatan). For double immuno-gold labeling, grids were rinsed 4x in TBS, blocked for 30 min in block buffer (1% BSA/TBS supplemented with 2.5 μg/ml gelatin, 2% BSAc), and incubated for 2 h in rabbit anti-TIA1 (1:500, Abcam cat#ab40693) and mouse anti-tau (Tau13 or TOC1, 1:1,000) antibodies diluted in block buffer. After 2 h, the grids were washed 4x in TBS prior to incubation for 1 h in 15 nm (anti-rabbit) and 6 nm (anti-mouse) gold particle-conjugated secondary antibodies diluted 1:50 in block buffer. After 1 h, the grids were washed 4x in TBS, then 2x with dH2O prior to treatment with 2% uranyl acetate. Grids were then washed a final 4x in dH2O and imaged as described above.
Apicco D.J., Ash P.E., Maziuk B., LeBlang C., Medalla M., Abdullatif A.A., Ferragud A., Botelho E., Ballance H.I., Dhawan U., Boudeau S., Cruz A.L., Kashy D., Wong A., Goldberg L.R., Yazdani N., Zhang C., Ung C.Y., Tripodis Y., Kanaan N.M., Ikezu T., Cottone P., Leszyk J., Li H., Luebke J., Bryant C.D, & Wolozin B. (2017). Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo. Nature neuroscience, 21(1), 72-80.
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4

Immunogold Labeling of Tau Aggregates

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Mixtures of tau aggregates were prepared using the ThioT aggregation assay described above. 48 h reaction mixtures with or without TIA1 were adsorbed for 2 min onto formvar/carbon-coated Nickel mesh grids, washed 2x with distilled water (dH20), treated with 2% uranyl acetate, washed 4x with dH20 and imaged at 80 kV using a JEOL JEM 1011 with a digital camera (Gatan). For double immuno-gold labeling, grids were rinsed 4x in TBS, blocked for 30 min in block buffer (1% BSA/TBS supplemented with 2.5 μg/ml gelatin, 2% BSAc), and incubated for 2 h in rabbit anti-TIA1 (1:500, Abcam cat#ab40693) and mouse anti-tau (Tau13 or TOC1, 1:1,000) antibodies diluted in block buffer. After 2 h, the grids were washed 4x in TBS prior to incubation for 1 h in 15 nm (anti-rabbit) and 6 nm (anti-mouse) gold particle-conjugated secondary antibodies diluted 1:50 in block buffer. After 1 h, the grids were washed 4x in TBS, then 2x with dH2O prior to treatment with 2% uranyl acetate. Grids were then washed a final 4x in dH2O and imaged as described above.
Apicco D.J., Ash P.E., Maziuk B., LeBlang C., Medalla M., Abdullatif A.A., Ferragud A., Botelho E., Ballance H.I., Dhawan U., Boudeau S., Cruz A.L., Kashy D., Wong A., Goldberg L.R., Yazdani N., Zhang C., Ung C.Y., Tripodis Y., Kanaan N.M., Ikezu T., Cottone P., Leszyk J., Li H., Luebke J., Bryant C.D, & Wolozin B. (2017). Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo. Nature neuroscience, 21(1), 72-80.
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