Phospho acc ser79

Manufactured by Merck Group

Phospho-ACC Ser79 is a laboratory reagent used to detect and quantify the phosphorylation of the Acetyl-CoA Carboxylase (ACC) enzyme at the serine 79 residue. This phosphorylation event is an important regulatory mechanism that inactivates the ACC enzyme, which plays a key role in fatty acid synthesis. The Phospho-ACC Ser79 reagent can be used in various biochemical and cell-based assays to study the regulation of lipid metabolism.

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Lab products found in correlation

Total akt, by Cell Signaling Technology (2 mentions) Ecl prime, by GE Healthcare (2 mentions) Ecl plus, by GE Healthcare (2 mentions) Phospho akt thr308, by Cell Signaling Technology (2 mentions) Phospho tbc1d1 thr590, by Cell Signaling Technology (2 mentions) Total acetyl coa carboxylase acc, by Cell Signaling Technology (2 mentions) Antibodies against phospho as160 thr642, by Merck Group (2 mentions) Phospho tbc1d1 ser237, by Merck Group (2 mentions) Hrp conjugated anti sheep igg, by Merck Group (2 mentions) Anti glut4antibody, by Bio-Rad (2 mentions) Phospho ampk thr172, by Cell Signaling Technology (2 mentions) Gradient gel, by Bio-Rad (2 mentions) Phenylmethylsulfonyl fluoride, by Thermo Fisher Scientific (2 mentions) Protease inhibitor cocktail, by Merck Group (2 mentions) Halt s phosphatase inhibitor, by Thermo Fisher Scientific (2 mentions) Enhanced chemi luminescence (ecl), by GE Healthcare (1 mentions) Hrp conjugated anti rabbit igg, by Thermo Fisher Scientific (1 mentions) Antibodies against phospho akt ser473, by Cell Signaling Technology (1 mentions) Total as160, by Merck Group (1 mentions) Srebp1, by BD (1 mentions)

Spelling variants of this product

Anti-phospho-ACC-Ser79 (2 citations)

4 protocols using phospho acc ser79

Antibody-based Analysis of Insulin Signaling

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Antibodies against phospho‐Akt Ser⁴⁷³ (#9271), phospho‐Akt
Thr³⁰⁸ (#9275), phospho‐TBC1D1 Thr⁵⁹⁰ (#6927), total Akt
(#9272), and total acetyl CoA carboxylase (ACC, #3662) were purchased from Cell
Signaling Technology (Beverly, MA). Antibodies against phospho‐AS160 Thr⁶⁴²(#07‐802), phospho‐ACC Ser⁷⁹ (#07‐303),
phospho‐TBC1D1 Ser²³⁷ (#07‐2268), and total AS160
(#07‐741) were from Millipore (Temecula, CA). Anti‐phospho‐AS160
Ser⁵⁸⁸(#3028P2) was from Symansis Limited (Timaru, New Zealand). Anti‐GLUT4
antibody (#4670‐1704) was from Bio‐Rad AbD Serotec (Oxford, UK).
HRP‐conjugated anti‐rabbit IgG was from Biosource International (Camarillo, CA).
HRP‐conjugated anti‐sheep IgG was from Millipore. Enhanced chemiluminescence reagents
(ECL, ECL Plus, and ECL Prime) were obtained from GE Healthcare Life Sciences (Uppsala, Sweden). All
other reagents were obtained from Sigma (St. Louis, MO).

Iwabe M., Kawamoto E., Koshinaka K, & Kawanaka K. (2014). Increased postexercise insulin sensitivity is accompanied by increased AS160 phosphorylation in slow‐twitch soleus muscle. Physiological Reports, 2(12), e12162.

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Western Blot Analysis of Hepatic Proteins

Cited 1 time

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Liver tissue samples were homogenized in RIPA buffer (50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1% IGEPAL, 0.5% w/v sodium deoxycholate and 0.1% w/v sodium dodecyl sulfate) with 1 mM phenylmethylsulfonyl fluoride (Thermo Fisher Scientific), protease inhibitor cocktail (Sigma) and Halt's phosphatase inhibitor (Thermo Fisher Scientific). Protein samples were subjected to SDS-PAGE using a 4–15% gradient gel (Bio-Rad), and transferred to a nitrocellulose membrane. Membranes were incubated overnight with primary antibodies against phospho-AMPK (Thr172) (Cell Signaling), phospho-ACC (Ser79) (Millipore), phospho-SREBP-1 (Cell Signaling), AMPK (Cell Signaling), ACC (Cell Signaling), SREBP-1 (BD Biosciences), SREBP-2 (Seo et al., 2011 (link)), β-actin (Sigma) and YY-1 (Cell Signaling), followed by HRP-conjugated secondary antibodies and chemiluminescent detection. Immunoblot intensities were quantified using ImageJ analysis software (Rasband, W.S., ImageJ, U. S. National Institutes of Health, Bethesda, Maryland, USA, https://imagej.nih.gov/ij/, 1997–2016).

Esquejo R.M., Salatto C.T., Delmore J., Albuquerque B., Reyes A., Shi Y., Moccia R., Cokorinos E., Peloquin M., Monetti M., Barricklow J., Bollinger E., Smith B.K., Day E.A., Nguyen C., Geoghegan K.F., Kreeger J.M., Opsahl A., Ward J., Kalgutkar A.S., Tess D., Butler L., Shirai N., Osborne T.F., Steinberg G.R., Birnbaum M.J., Cameron K.O, & Miller R.A. (2018). Activation of Liver AMPK with PF-06409577 Corrects NAFLD and Lowers Cholesterol in Rodent and Primate Preclinical Models. EBioMedicine, 31, 122-132.

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Signaling Pathway Protein Detection

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Antibodies against phospho‐Akt Ser⁴⁷³ (#9271), phospho‐Akt Thr³⁰⁸ (#9275), phospho‐TBC1D1 Thr⁵⁹⁰ (#6927), phospho‐JNK Thr¹⁸³/Tyr¹⁸⁵ (#9251), phospho‐p38 MAPK Thr¹⁸⁰/Tyr¹⁸² (#9216), phospho‐ERK1/2 Thr²⁰²/Tyr²⁰⁴ (#9101), total Akt (#9272), total TBC1D1 (#4629S), total‐JNK (#9252), total‐p38 MAPK (#9212), total‐ERK1/2 (#9102), total IκBα (#9242), and total‐acetyl CoA carboxylase (ACC, #3662) were from Cell Signaling Technology (Beverly, MA). Antibodies against phospho‐AS160 Thr⁶⁴² (#07‐802), phospho‐ACC Ser⁷⁹ (#07‐303), phospho‐TBC1D1 Ser²³⁷ (#07‐2268), and total AS160 (#07‐741) were from Millipore (Temecula, CA). Anti‐phospho‐AS160 Ser⁵⁸⁸ (#3028P2) was from Symansis Limited (Timaru, New Zealand). Anti‐GLUT4 antibody (#4670‐1704) was from Bio‐Rad AbD Serotec (Oxford, UK). Anti‐SPT2 antibody (ab23696) was from Abcam (Cambridge, MA). Horseradish peroxidase (HRP)‐conjugated anti‐rabbit IgG was from Biosource International (Camarillo, CA). HRP‐conjugated anti‐sheep IgG was from Millipore. HRP‐conjugated anti‐mouse IgG was from Santa Cruz Biotechnology. Enhanced chemiluminescence reagents (ECL, ECL plus, and ECL Prime) were obtained from GE Healthcare Life Sciences (Uppsala, Sweden). All other reagents were obtained from Sigma‐Aldrich (St. Louis, MO).

Kawamoto E., Koshinaka K., Yoshimura T., Masuda H, & Kawanaka K. (2016). Immobilization rapidly induces muscle insulin resistance together with the activation of MAPKs (JNK and p38) and impairment of AS160 phosphorylation. Physiological Reports, 4(15), e12876.

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AMPK Signaling Pathway Activation

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To measure AMPK signaling, EDL muscle fibers were incubated in an oxygenated Buffer A bath for 5 min. Buffer A was aspirated and replaced with fresh Buffer A containing DMSO (vehicle), PF-739 (10 μM). A subset of muscle fibers treated with vehicle were contracted by electrical pulsation for 30 min. EDL muscle fibers were stored in a tube and immediately snap frozen in liquid nitrogen. For western blotting, EDL muscle fibers were homogenized in RIPA buffer (50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1% IGEPAL, 0.5% w/v sodium deoxycholate and 0.1% w/v sodium dodecyl sulfate) with 1 mM phenylmethylsulfonyl fluoride (Thermo Fisher Scientific), protease inhibitor cocktail (Sigma) and Halt’s phosphatase inhibitor (Thermo Fisher Scientific). Protein samples were subjected to SDS-PAGE using a 4–15% gradient gel (Bio-Rad), and transferred to a nitrocellulose membrane. Membranes were incubated overnight with primary antibodies against phospho-AMPK (Thr172) (Cell Signaling, Cat# 2535S), phospho-ACC (Ser79) (Millipore, Cat#07–303), phospho-TBC1D1 (Millipore Cat#07–2268), pan-AMPKα (Cell Signaling, Cat #5831S), ACC (Cell Signaling, Cat#3662S), TBC1D1 (Cell Signaling, Cat#4629S), and α-tubulin (Cell Signaling, Cat#2125S), followed by HRP-conjugated secondary antibodies and chemiluminescent detection.

Esquejo R.M., Albuquerque B., Sher A., Blatnik M., Wald K., Peloquin M., Delmore J., Kindt E., Li W., Young J.D., Cameron K, & Miller R.A. (2022). AMPK activation is sufficient to increase skeletal muscle glucose uptake and glycogen synthesis but is not required for contraction-mediated increases in glucose metabolism. Heliyon, 8(10), e11091.

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