- PA5-17831 - Invitrogen Antibodies PRKAA2 antibody

Submitted references The combination of lactoferrin and linolenic acid inhibits colorectal tumor growth through activating AMPK/JNK-related apoptosis pathway.

Yao Q, Li H, Fan L, Huang S, Wang J, Zheng N
PeerJ 2021;9:e11072

SIRT6 enhances oxidative phosphorylation in breast cancer and promotes mammary tumorigenesis in mice.

Becherini P, Caffa I, Piacente F, Damonte P, Vellone VG, Passalacqua M, Benzi A, Bonfiglio T, Reverberi D, Khalifa A, Ghanem M, Guijarro A, Tagliafico L, Sucameli M, Persia A, Monacelli F, Cea M, Bruzzone S, Ravera S, Nencioni A
Cancer & metabolism 2021 Jan 22;9(1):6

Mitochondria as Target for Tumor Management of Hemangioendothelioma.

Gordillo GM, Biswas A, Singh K, Sen A, Guda PR, Miller C, Pan X, Khanna S, Cadenas E, Sen CK
Antioxidants & redox signaling 2021 Jan 10;34(2):137-153

Fasting-mimicking diet and hormone therapy induce breast cancer regression.

Caffa I, Spagnolo V, Vernieri C, Valdemarin F, Becherini P, Wei M, Brandhorst S, Zucal C, Driehuis E, Ferrando L, Piacente F, Tagliafico A, Cilli M, Mastracci L, Vellone VG, Piazza S, Cremonini AL, Gradaschi R, Mantero C, Passalacqua M, Ballestrero A, Zoppoli G, Cea M, Arrighi A, Odetti P, Monacelli F, Salvadori G, Cortellino S, Clevers H, De Braud F, Sukkar SG, Provenzani A, Longo VD, Nencioni A
Nature 2020 Jul;583(7817):620-624

Expression and Impact of Vaspin on In Vitro Oocyte Maturation through MAP3/1 and PRKAA1 Signalling Pathways.

Kurowska P, Mlyczyńska E, Estienne A, Barbe A, Rajska I, Soból K, Poniedziałek-Kempny K, Dupont J, Rak A
International journal of molecular sciences 2020 Dec 8;21(24)

C‑type natriuretic peptide prevents angiotensin II‑induced atrial connexin 40 and 43 dysregulation by activating AMP‑activated kinase signaling.

Ding DZ, Jia YN, Zhang B, Guan CM, Zhou S, Li X, Cui X
Molecular medicine reports 2019 Dec;20(6):5091-5099

Cryptotanshinone from the Salvia miltiorrhiza Bunge Attenuates Ethanol-Induced Liver Injury by Activation of AMPK/SIRT1 and Nrf2 Signaling Pathways.

Nagappan A, Kim JH, Jung DY, Jung MH
International journal of molecular sciences 2019 Dec 30;21(1)

Gomisin N Alleviates Ethanol-Induced Liver Injury through Ameliorating Lipid Metabolism and Oxidative Stress.

Nagappan A, Jung DY, Kim JH, Lee H, Jung MH
International journal of molecular sciences 2018 Sep 1;19(9)

Trehalose 6-Phosphate Positively Regulates Fatty Acid Synthesis by Stabilizing WRINKLED1.

Zhai Z, Keereetaweep J, Liu H, Feil R, Lunn JE, Shanklin J
The Plant cell 2018 Oct;30(10):2616-2627

Palmitoleic acid reduces intramuscular lipid and restores insulin sensitivity in obese sheep.

Duckett SK, Volpi-Lagreca G, Alende M, Long NM
Diabetes, metabolic syndrome and obesity : targets and therapy 2014;7:553-63

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Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot analysis was performed on whole cell extracts (30 µg lysate) of A-431 (Lane 1), A-431 treated with Metformin (10mM for 24 h) (Lane 2), Hep G2 (Lane 3), Hep G2 treated with Metformin (10mM for 24 h) (Lane 4), U-87 MG (Lane 5), and U-87 MG treated with AICAR (1mM for 48 h) (Lane 6). The blot was probed with Phospho-AMPK alpha-1,2 (Thr183, Thr172) Monoclonal Antibody (Product # PA5-17831, 1:1000 dilution) and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal™ Secondary Antibody, HRP conjugate (Product # A27036, 0.25 µg/mL, 1:4000 dilution). A 63 kDa band corresponding to Phospho-AMPK alpha-1 (Thr172) was observed across the cell lines tested and enhanced upon treatment.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot analysis of Phospho-AMPK-alpha 1,2 (Thr183, Thr172) was performed by loading 30 µg of THP-1 cell lysates from cells either treated with a vehicle control (C, left lane) or with 100 nM PMA (right lane) for 15 minutes, onto an SDS-PAGE gel. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat dry milk in TBST for 1 hour at room temperature. The membrane was probed with a Phospho-AMPK alpha-1,2 (Thr183, Thr172) polyclonal antibody (Product # PA5-17831) at a dilution of 1:1000 for overnight at 4°C, washed in TBST, and probed with an HRP-conjugated goat anti-rabbit IgG at a dilution of 1:40,000 for 1 hour at room temperature. Detection was performed using ECL substrate. Data courtesy of the Innovators Program.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot analysis was performed on whole cell extracts (30 µg lysate) of A-431 (Lane 1), A-431 treated with Metformin (10mM for 24 h) (Lane 2), Hep G2 (Lane 3), Hep G2 treated with Metformin (10mM for 24 h) (Lane 4), U-87 MG (Lane 5), and U-87 MG treated with AICAR (1mM for 48 h) (Lane 6). The blot was probed with Phospho-AMPK alpha-1,2 (Thr183, Thr172) Monoclonal Antibody (Product # PA5-17831, 1:1000 dilution) and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal™ Secondary Antibody, HRP conjugate (Product # A27036, 0.25 µg/mL, 1:4000 dilution). A 63 kDa band corresponding to Phospho-AMPK alpha-1 (Thr172) was observed across the cell lines tested and enhanced upon treatment.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 4 Effect of vaspin on mitogen-activated kinase (MAP3/1) and AMP-activated kinase (PRKAA1) phosphorylation in oocytes and cumulus cells after in vitro maturation. COCs (50/group/experiment) were selected after morphological examination of material collected from the ovaries taken from 100 pigs (15 follicles/ovary). Porcine cumulus-oocyte complex (COCs) were cultured for 44 h in maturation medium in the presence or absence of vaspin (1 ng/mL) then mechanically separated into oocytes and cumulus cells. Phospho MAP3/1 (pMAP3/1), MAP3/1 ( A ) and phospho PRKAA1 (pPRKAA1), PRKAA1 ( B ) protein expressions were analysed by Western blot analysis. Protein expression levels were normalised to actin. Experiments were performed independently and repeated three times ( n = 3). Data are plotted as the mean +- SEM of three independent experiments. Significance between control and vaspin is indicated by ** p < 0.01 and *** p < 0.001.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Fig. 3 SIRT6 enhances OXPHOS and energy status in MDA-MB-231 cells. a - h Expression ( a ) and activity ( b ) of pyruvate dehydrogenase (PDH), activity of mitochondrial complexes ( c - e ), oxygen consumption ( f ), activity of F o -F 1 ATP synthase ( g ), and energy status, expressed as ATP/AMP ratio ( h ), were measured in MDA-MB-231 cells transduced with human WT or catalytically inactive (H133Y) SIRT6, or with a control vector (VECTOR). Data are presented as mean +- SD of three different experiments. * P < 0.05, ** P < 0.01, *** P < 0.001; ns, not statistically significant. i - p Expression ( i ) and activity ( j ) of PDH, activity of mitochondrial complexes ( k - m ), oxygen consumption ( n ), activity of F o -F 1 ATP synthase ( o ), and energy status, expressed as ATP/AMP ratio ( p ) were measured in MDA-MB-231 cells transduced with a short hairpin RNA targeting SIRT6 or with a control vector (VECTOR). Data are presented as mean +- SD of three different experiments. ** P < 0.01, *** P < 0.001. q 2 x 10 6 MDA-MB-231 BC cells transduced with either a SIRT6-shRNA or a control vector (VECTOR) were injected subcutaneously in both flanks of BALB/c athymic nude mice. Mice were sacrificed, and tumors were excised 50 days after cell inoculation. Proteins were extracted, and phosphorylated AMPK (Thr183, Thr172), total AMPK, and vinculin were detected by Western blot. One representative experiment out of two is presented

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Additional file 5: Fig. S5. SIRT6 silencing enhances AMPK phosphorylation in MDA-MB-231 xenografts. A, MDA-MB-231 cells were engineered to express a SIRT6-shRNA (or a control vector). Thereafter, cells were used for protein lysate generation and phosphorylated AMPK (Thr183, Thr172), total AMPK and GAPDH were detected by Western blot. One representative experiment out of three is presented. B, MDA-MB-231 BC cells transduced with either a SIRT6-shRNA or with a control vector were injected subcutaneously into both flanks of BALB/c athymic nude mice. Animals were sacrificed 50 days after cell inoculation; tumors were used for protein lysate generation and phosphorylated and total AMPK, SIRT6 and vinculin were detected by Western blot. In the right panel, the intensity of the phospho-AMPK bands was normalized to that of the total AMPK bands and the phospho-AMPK/total-AMPK ratio in tumors with silenced SIRT6 was compared to that detected in control tumors. Data are presented as mean +- SD. * p

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 5 Gomisin N prevents ethanol-mediated reduction in sirtuin1 (SIRT1) and phosphorylated AMP-kinase (AMPK) in the liver of chronic-binge ethanol-fed mice. ( A ) Western blot analysis of SIRT1. Representative images are shown ( left ). SIRT1 level was quantified by densitometry ( right ). ( B ) Western blot analysis of p-AMPK and acetyl-CoA carboxylase (p-ACC). Representative images are shown ( left ). Levels of p-AMPK and p-ACC were quantified by densitometry ( right ). Values are the mean +- SD ( n = 6). # p < 0.01, ## p < 0.01 vs. pair-fed control mice, * p < 0.05, ** p < 0.01 vs. ethanol-fed mice.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 9 Gomisin N reverses ethanol-mediated reduction in SIRT1 and phosphorylated AMPK in HepG2 cells. HepG2 cells were treated with 50 mM ethanol in the presence or absence of GN (50 or 100 muM) for 24 h. ( A ) Western blot analysis of SIRT1. ( B ) Western blot analysis of p-AMPK and p-ACC. ( C ) Measurement of NAD + /NADH ratio. ( D ) HepG2 cells were pretreated with GN (100 muM) for 3 h or with Ex52735 (10 muM) for 6 h and then treated with ethanol (100 muM). Measurement of intracellular TG levels. Values are the mean +- SD of triplicate experiments. # p < 0.05, ## p < 0.01 vs. untreated control, * p < 0.05, ** p < 0.01 vs. ethanol-treated group. SS p < 0.05 vs. ethanol and GN-treated group.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 7. Effects of CNP and cANP 4-23 , an agonist of NPR-C, on the regulation of atrial p-AMPK expression. Data were expressed as mean +- standard error of the mean; n=5. *P

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 5 CT activated AMPK/SIRT1 signaling. ( A , B ) HepG2 cells were treated with 2.5 muM CT for indicated times. Western blot analysis of phosphorylated AMPK , ACC , SIRT1 , and Nrf2 . ( C ) C57BL/6 mice were pair-fed either control or ethanol-containing diet with or without CT (20 or 40 mg/kg) for four weeks. Western blot analysis of phosphorylated AMPK , SIRT1. CYP2E1 , and Nrf2 . ( D ) HepG2 cells were incubated with 50 mM ethanol and treated with CT (2.5 or 5 muM) for 24 h. Western blot analysis of phosphorylated AMPK , SIRT1 , CYP2E1 , and Nrf2 . ( E ) AML-12 cells were incubated with 50 mM ethanol and treated with CT (2.5 or 5 muM) for 24 h. Western blot analysis of phosphorylated AMPK and SIRT1 . The images are representative ( F ) HepG2 cells were pretreated with CT (2.5 muM) for 3 h or with compound C (comp C) (10 muM) for 6 h, followed by ethanol (100 muM) treatment. Measurement of intracellular TG levels. Data are shown as mean +- SD of three independent experiments. # p < 0.05 vs. untreated control, ** p < 0.01 vs. ethanol-treated group. SS SS p < 0.01 vs. ethanol and CT-treated group. Densitometric analysis of western blots are given in Supplementary Figures S2 and S3A-G .

PA5-17831

Antibody data