Anti pep12

Manufactured by Thermo Fisher Scientific

Anti-Pep12 is a laboratory product designed for use in biological research. It functions as an antibody that specifically binds to the Pep12 protein, which is involved in cellular processes. The core purpose of Anti-Pep12 is to facilitate the study and analysis of the Pep12 protein and its associated biological mechanisms.

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Lab products found in correlation

Anti dpm1, by Thermo Fisher Scientific (3 mentions) Anti pgk1, by Thermo Fisher Scientific (2 mentions) Hrp conjugated anti mouse or anti rabbit igg secondary antibodies, by Merck Group (1 mentions) Anti ha, by Roche (1 mentions) Luminata forte western hrp substrate, by Merck Group (1 mentions) Anti pma1, by Abcam (1 mentions) Anti phospho p44 42 mapk, by Cell Signaling Technology (1 mentions) Anti glucose 6 phosphate dehydrogenase g 6 pdh, by Merck Group (1 mentions) Anti gfp, by Santa Cruz Biotechnology (1 mentions) Anti myc, by Roche (1 mentions) Anti porin, by Thermo Fisher Scientific (1 mentions) Anti phospho ser thr ampk substrate, by Cell Signaling Technology (1 mentions) Anti histone h4, by Abcam (1 mentions) Anti ha, by Abmart (1 mentions) Anti phospho ampka thr172, by Cell Signaling Technology (1 mentions) Anti actin, by Abmart (1 mentions) Anti atr, by Santa Cruz Biotechnology (1 mentions) Anti flag, by Merck Group (1 mentions) Anti gfp, by Roche (1 mentions) Anti cox 2, by Thermo Fisher Scientific (1 mentions)

5 protocols using anti pep12

Antibody Immunoblot Analysis

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Anti-HA and anti-Ubiquitin were purchased from Roche and BioMol, respectively. Anti-Sec61 antibody was a generous gift from Jeffrey L. Brodsky (University of Pittsburgh, Pittsburgh, PA). Anti-Kex2 and anti-Pma1 antibodies were purchased from Abcam. Anti-Pep12, anti-Dpm1, anti-Pho8, and anti-Pgk1 antibodies were purchased from Invitrogen. Immunoblots were incubated with the indicated primary antibodies and appropriate HRP-conjugated anti-mouse or anti-rabbit IgG secondary antibodies (Sigma). The HRP-chemiluminescent signal was visualized by enhanced chemiluminescence (Pierce, USA) or Luminata Forte Western HRP substrate (Millipore).

Nakatsukasa K, & Kamura T. (2016). Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated Degradation. PLoS ONE, 11(2), e0148327.

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Immunoblot Analysis of Yeast Signaling

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Cells were mechanically lysed in the presence of phosphatase inhibitors. Extracts were analyzed by SDS–PAGE and immunoblotting with the following antibodies: anti-Pep12 (Invitrogen, Thermo Fisher Scientific, Waltham, MA), anti–glucose-6-phosphate dehydrogenase (G6PDH; Sigma-Aldrich, St. Louis, MO), anti–phosphoglycerate kinase (PGK; Novex, Thermo Fisher Scientific, Waltham, MA), anti-GFP (Santa Cruz Biotechnology, Dallas, TX, or Roche, Burgess Hill, UK), anti-PKC (pan) zeta T410 (Cell Signaling, Danvers, MA) for phospho-Ypk1(T504), anti-phospho-Ypk1(T662) (Niles et al., 2012 (link)), anti-Ypk1 (Cell Signaling), and anti–phospho-p44/42 MAPK (Cell Signaling) for phospho-Slt2. Levels of GFP-Pkh1, Ypk1, phospho-Ypk1, and phospho-Slt2 were normalized to protein loading controls (Pep12, G6PDH, or PGK). See the Supplemental Materials and Methods for additional details.

Omnus D.J., Manford A.G., Bader J.M., Emr S.D, & Stefan C.J. (2016). Phosphoinositide kinase signaling controls ER-PM cross-talk. Molecular Biology of the Cell, 27(7), 1170-1180.

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Antibody Validation and Dilution Protocol

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Antibodies were purchased as follows and used at the indicated dilutions: anti-GFP (Roche, 11814460001, 1:2500), anti-MYC (Roche, 11667149001, 1:2500), anti-HA (Abmart, M20003L, 1:2500), anti-FLAG (Sigma, F1804, 1:2500), anti-phospho-AMPKa (Thr172) (Cell Signaling Technology, 2535S, 1:1000), anti-Phospho-(Ser/Thr) AMPK Substrate (Cell Signaling Technology, 5759S, 1: 1000), anti-PGK1 (Nordic Immunology, NE130/7S, 1:10000), anti-Dpm1 (Invitrogen, A6429, 1:2000), anti-ALP (Invitrogen, A6458, 1:2000), anti-Pep12 (Invitrogen, A21273, 1:2000), anti-Porin (Invitrogen, A6449, 1:20000), anti-Histone H4 (Abcam, Ab10158, 1:2500), anti-LC3 (MBL, PM036, 1:1000), anti-ATR (Santa Cruz, SC-1887, 1:250), anti-Actin (Abmart, P30002, 1:5000). Goat Anti-Mouse IgG1, Human ads-HRP (SouthernBiotech, 1070-05, 1:10000) and Goat Anti-Rabbit IgG, Human ads-HRP (SouthernBiotech, 4010-05, 1:10000).

Yi C., Tong J., Lu P., Wang Y., Zhang J., Sun C., Yuan K., Xue R., Zou B., Li N., Xiao S., Dai C., Huang Y., Xu L., Li L., Chen S., Miao D., Deng H., Li H, & Yu L. (2017). Formation of a Snf1-Mec1-Atg1 Module on Mitochondria Governs Energy Deprivation-Induced Autophagy by Regulating Mitochondrial Respiration. Developmental cell, 41(1).

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Organelle Marker Immunoblotting

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Fractionation was performed as described previously [41 (link)]. Anti-Pgk1 (Molecular probes), anti-Pep12 (Molecular probes), anti-Sed5 (provided by Koji Yoda), anti-CPY (provided by Akihiko Nakano), anti-Dpm1 (Molecular probes), and anti-Cox2 (Invitrogen) antibodies were used for organelle markers for the cytosol, endosome, Golgi apparatus, vacuole, endoplasmic reticulum, and mitochondria, respectively.

Mizuike A., Kobayashi S., Rikukawa T., Ohta A., Horiuchi H, & Fukuda R. (2019). Suppression of respiratory growth defect of mitochondrial phosphatidylserine decarboxylase deficient mutant by overproduction of Sfh1, a Sec14 homolog, in yeast. PLoS ONE, 14(4), e0215009.

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Immunoblotting Analysis of Protein Purification

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At each step in the purification, 10% each of the crude lysate, S5, P5, FT was stored 1:1 in 2X Tris-Glycine sample buffer at −80°C. The samples were subjected to standard immunoblotting procedures. Primary antibodies used: a custom rabbit polyclonal anti-GFP; mouse anti-PMA-1 (Molecular Probes, 40B7); rabbit polyclonal anti-Pep12 (Molecular Probes, 710037). Secondary antibodies: horseradish peroxidase-coupled goat anti-rabbit or sheep anti-mouse antibodies. The blots were developed with ECL substrates and imaged in a BioRad ChemiDoc Touch system.

Jin M., Fuller G.G., Han T., Yao Y., Alessi A.F., Freeberg M.A., Roach N., Moresco J.J., Karnovsky A., Baba M., Yates JR I.I.I., Gitler A.D., Inoki K., Klionsky D.J, & Kim J.K. (2017). Glycolytic Enzymes Coalesce in G bodies Under Hypoxic Stress. Cell reports, 20(4), 895-908.

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