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Rabbit anti akt pt308

Manufactured by Cell Signaling Technology
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Rabbit anti-Akt-pT308 is a primary antibody that specifically recognizes the phosphorylated threonine 308 residue of the Akt protein. It is intended for use in various analytical techniques, such as Western blotting, to detect and quantify the phosphorylation level of the Akt protein at the threonine 308 site.

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Lab products found in correlation

Anti v5 r960 25, by Thermo Fisher Scientific (2 mentions) Anti ps473 akt, by Cell Signaling Technology (2 mentions) Anti nedd4l 13690 1 ap, by Proteintech (2 mentions) P s6s236 236, by Cell Signaling Technology (2 mentions) Anti ub sc 8017, by Santa Cruz Biotechnology (2 mentions) Protein assay reagent, by Bio-Rad (2 mentions) Anti pan akt, by Cell Signaling Technology (2 mentions) Anti s6, by Cell Signaling Technology (2 mentions) Phosphatases inhibitors, by Merck Group (2 mentions) Protease inhibitor, by Roche (2 mentions) Mouse anti α tubulin, by Abcam (1 mentions) Rabbit anti akt, by Cell Signaling Technology (1 mentions) Mouse anti β actin, by Proteintech (1 mentions) Rabbit anti akt ps473, by Cell Signaling Technology (1 mentions) Veriblot for ip secondary antibody, by Abcam (1 mentions)

Close spelling variants of this product

Anti-pT308 Akt PT308-AKT Rabbit anti-AKT Anti-AKT

3 protocols using rabbit anti akt pt308

1

Sperm Phosphorylation Pathway Analysis

Cited 1 time
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The phosphorylation levels of PHB and the PI3K/AKT pathway in mouse sperm after treatment with wortmannin, and in human sperm with reduced motility from infertile males, were measured using western blotting analysis as previously described.5 (link)6 (link) The following primary antibodies were used: rabbit anti-PHB pT258 (1:500, GTX55299, GeneTex); rabbit anti-PI3 Kinase p85 (1:500, #4292), rabbit anti-AKT (1:500, #4060), rabbit anti-AKT pT308 (1:500, #9275) and rabbit anti-AKT pS473 (1:500, #9272) purchased from Cell Signaling Technology; rabbit anti-PI3K p85 alpha+gamma (Phospho Y199+Y467; 1:500, ab196001) and rabbit anti-PHB (1:500, ab75766) from Abcam; mouse anti-α-tubulin (1:1000, 66031-1-Ig) and mouse anti-β-actin (1:1000, 60008-1-Ig) from Proteintech Group, Inc. (Rosemont, IL, USA). To block the interference of IgG heavy and light chains on IP lysate blotting, a specific IP secondary antibody (the VeriBlot for IP secondary antibody [horseradish peroxidase, HRP; 1:40, ab131366]) purchased from Abcam was applied to detect the bound protein in the IP lysate. Images were captured using a Fujifilm LAS-4000 Mini Luminescent Imaging Analyzer (Fuji Film, Tokyo, Japan). The band intensities were quantified with ImageJ Software (National Institutes of Health, Bethesda, MA, USA).
Li X.H., Chai R.R., Chen G.W., Zhang L.F., Tan-Tai W.J., Shi H.J., Martin-DeLeon P.A., Wai-Sum O, & Chen H. (2020). Prohibitin (PHB) interacts with AKT in mitochondria to coordinately modulate sperm motility. Asian Journal of Andrology, 22(6), 583-589.
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2

Protein Extraction and Western Blot Analysis

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Cells were lysed in RIPA buffer (50mM Tris HCl, pH 7.7; 0.15M NaCl; 1mM EDTA; 1% Triton X-100) supplemented with protease inhibitors (Roche) and phosphatases inhibitors (Sigma Aldrich). Protein concentration was measured using Bio-Rad protein assay reagent (Biorad Laboratories, CA). Samples were denatured at 95°C for 10 min in loading buffer then resolved in SDS-PAGE and transferred onto nitrocellulose membranes. Membranes were then blocked in 5% non-fat milk in TBS buffer, 0.1% Tween and then immunoblotted using the following primary antibodies in the specified concentrations: anti-Nedd4l (13690-1-AP, rabbit, Proteintech, 1:1000), anti-Actin (mouse, IGBMC, 1:1000), anti-Akt-pS473 (#4060, rabbit, Cell Signalling, 1:1000), rabbit anti-Akt-pT308 (#2965, rabbit, Cell Signalling, 1:1000) anti-Akt (pan) (#4691, rabbit, Cell Signalling, 1:1000), p-S6S236/236 (#2211, rabbit, Cell Signalling, 1/1000), anti-S6 (#2217, rabbit, Cell Signalling, 1:1000), anti-Ub (sc-8017, mouse, Santa Cruz, 1:250), anti-V5 (R96025, mouse, Invitrogen, 1:5000). All WB experiments consist of at least 3 independent replicates.
Broix L., Jagline H., Ivanova E., Schmucker S., Drouot N., Clayton-Smith J., Pagnamenta A.T., Metcalfe K.A., Isidor B., Louvier U.W., Poduri A., Taylor J.C., Tilly P., Poirier K., Saillour Y., Lebrun N., Stemmelen T., Rudolf G., Muraca G., Saintpierre B., Elmorjani A., Moïse M., Weirauch N.B., Guerrini R., Boland A., Olaso R., Masson C., Tripathy R., Keays D., Beldjord C., Nguyen L., Godin J., Kini U., Nischké P., Deleuze J.F., Bahi-Buisson N., Sumara I., Hinckelmann M.V, & Chelly J. (2016). Mutations in the HECT domain of NEDD4L lead to AKT/mTOR pathway deregulation and cause periventricular nodular heterotopia. Nature genetics, 48(11), 1349-1358.
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3

Protein Extraction and Western Blot Analysis

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Cells were lysed in RIPA buffer (50mM Tris HCl, pH 7.7; 0.15M NaCl; 1mM EDTA; 1% Triton X-100) supplemented with protease inhibitors (Roche) and phosphatases inhibitors (Sigma Aldrich). Protein concentration was measured using Bio-Rad protein assay reagent (Biorad Laboratories, CA). Samples were denatured at 95°C for 10 min in loading buffer then resolved in SDS-PAGE and transferred onto nitrocellulose membranes. Membranes were then blocked in 5% non-fat milk in TBS buffer, 0.1% Tween and then immunoblotted using the following primary antibodies in the specified concentrations: anti-Nedd4l (13690-1-AP, rabbit, Proteintech, 1:1000), anti-Actin (mouse, IGBMC, 1:1000), anti-Akt-pS473 (#4060, rabbit, Cell Signalling, 1:1000), rabbit anti-Akt-pT308 (#2965, rabbit, Cell Signalling, 1:1000) anti-Akt (pan) (#4691, rabbit, Cell Signalling, 1:1000), p-S6S236/236 (#2211, rabbit, Cell Signalling, 1/1000), anti-S6 (#2217, rabbit, Cell Signalling, 1:1000), anti-Ub (sc-8017, mouse, Santa Cruz, 1:250), anti-V5 (R96025, mouse, Invitrogen, 1:5000). All WB experiments consist of at least 3 independent replicates.
Broix L., Jagline H., Ivanova E., Schmucker S., Drouot N., Clayton-Smith J., Pagnamenta A.T., Metcalfe K.A., Isidor B., Louvier U.W., Poduri A., Taylor J.C., Tilly P., Poirier K., Saillour Y., Lebrun N., Stemmelen T., Rudolf G., Muraca G., Saintpierre B., Elmorjani A., Moïse M., Weirauch N.B., Guerrini R., Boland A., Olaso R., Masson C., Tripathy R., Keays D., Beldjord C., Nguyen L., Godin J., Kini U., Nischké P., Deleuze J.F., Bahi-Buisson N., Sumara I., Hinckelmann M.V, & Chelly J. (2016). Mutations in the HECT domain of NEDD4L lead to AKT/mTOR pathway deregulation and cause periventricular nodular heterotopia. Nature genetics, 48(11), 1349-1358.
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