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Anti p lats

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Anti-p-LATS is a primary antibody that recognizes the phosphorylated form of the LATS protein. LATS, or Large Tumor Suppressor, is a key regulator in the Hippo signaling pathway. The Anti-p-LATS antibody can be used to detect and quantify the phosphorylation state of LATS in various experimental systems.

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Lab products found in correlation

Anti p yap, by Cell Signaling Technology (4 mentions) Anti yap, by Cell Signaling Technology (3 mentions) Anti lat, by Cell Signaling Technology (3 mentions) Anti lats1, by Cell Signaling Technology (2 mentions) Anti actin, by Merck Group (2 mentions) Anti p mst, by Cell Signaling Technology (2 mentions) Anti yap taz, by Santa Cruz Biotechnology (2 mentions) Anti gapdh, by Merck Group (2 mentions) Anti p mlc2, by Cell Signaling Technology (1 mentions) Anti mlc2, by Cell Signaling Technology (1 mentions) Anti c myc, by Abcam (1 mentions) Anti lamin b, by Santa Cruz Biotechnology (1 mentions) Anti hmgcr, by Santa Cruz Biotechnology (1 mentions) Anti myc tag, by Cell Signaling Technology (1 mentions) Anti bnip3, by Santa Cruz Biotechnology (1 mentions) Anti hif 1α, by BD (1 mentions) Anti β actin, by BD (1 mentions) Anti β catenin, by Merck Group (1 mentions) Anti axin2, by Cell Signaling Technology (1 mentions) Anti yap taz, by Cell Signaling Technology (1 mentions)

6 protocols using anti p lats

1

Western Blot Analysis of Cell Signaling

Cited 1 time
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Cultured cells were lysed and analyzed. Primary antibodies used for Western blot were rabbit anti-MLC2 (1:1000; Cell Signaling, 8505), anti-p-MLC2 (1:1000; Cell Signaling, 3674), anti-Lats1 (1:1000; Cell Signaling, 3477), anti-p-Lats (Yu et al. 2010 (link)), anti-YAP (1:1000; Cell Signaling, 4912), anti-p-S397-YAP (1:1000; Cell Signaling, 13619), and anti-c-Myc (1:1000; Abcam, ab32072) and mouse anti-RhoA (1:500; Cytoskeleton, Inc., ARH03) and anti-Actin (1:20,000; Millipore, MAB1501R).
Cai J., Song X., Wang W., Watnick T., Pei Y., Qian F, & Pan D. (2018). A RhoA–YAP–c-Myc signaling axis promotes the development of polycystic kidney disease. Genes & Development, 32(11-12), 781-793.
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2

Immunoblotting Protein Analysis in Cells

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Immunobloting analysis of proteins in cell lysates and nuclear fractions was performed as previously described [56 (link), 57 (link)]. Primary antibodies used were as follows: anti-YAP (#4912), anti-p-YAP (#4911), anti-Myc-Tag (#2278), anti-Mst (#3682), anti-p-Mst (#3681), anti-LATS (#3477) and anti-p-LATS (#8654) were purchased from Cell Signaling Technology (Beverly, MA); anti-HIF-1α (#610959) was purchased from BD; anti-β-Actin (#Sc-47778), anti-Lamin B (#Sc-6216), anti-BNIP3 (#Sc-56167), and anti-HMGCR (#27578) were purchased from Santa Cruz (Santa Cruz, CA).
Dai X.Y., Zhuang L.H., Wang D.D., Zhou T.Y., Chang L.L., Gai R.H., Zhu D.F., Yang B., Zhu H, & He Q.J. (2016). Nuclear translocation and activation of YAP by hypoxia contributes to the chemoresistance of SN38 in hepatocellular carcinoma cells. Oncotarget, 7(6), 6933-6947.
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3

Immunoblotting Protocol Verification

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Immunoblots were carried out as previously described52 (link). Primary antibodies used were: anti-YAP/TAZ (Santa Cruz Biotechnology, sc-101199), anti-P-YAP (Cell Signaling Technology, 4911), anti-LATS (Cell Signaling Technology, 3477), anti-p-LATS (Cell Signaling Technology, 8654) and anti-GAPDH (Millipore, MAB374). Uncropped immunoblots are presented in Supplementary Figure 1.
Panciera T., Citron A., Di Biagio D., Battilana G., Gandin A., Giulitti S., Forcato M., Bicciato S., Panzetta V., Fusco S., Azzolin L., Totaro A., Dei Tos A.P., Fassan M., Vindigni V., Bassetto F., Rosato A., Brusatin G., Cordenonsi M, & Piccolo S. (2020). Reprogramming normal cells into tumor precursors requires ECM stiffness and oncogene-mediated changes of cell mechanical properties. Nature materials, 19(7), 797-806.
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4

Western Blot Analysis of Hippo-YAP Pathway

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Jejunal tissues and cultured cells were lysed, and the extracted proteins were analyzed. The primary antibodies used for Western blot were rabbit anti-Mst1 (1:1000; Cell Signaling), anti-p-Mst (1:1000; Cell Signaling), anti-Lats1 (1:1000; Cell Signaling), anti-p-Lats (Yu et al. 2010 (link)), anti-YAP (1:1000 [Cell Signaling, #4912], 1:1000 [Santa Cruz Biotechnology, H-9 and 63.7], and 1:1000 [Novus, NB110-58358]), anti-p-YAP (S127; 1:1000; Cell Signaling), anti-p-YAP (S381; 1:1000; Cell Signaling) (Kim et al. 2013 (link)), anti-β-catenin (1:2500; Sigma), anti-YAP/TAZ (1:1000; Cell Signaling), anti-Axin2 (1:1000; Cell Signaling), mouse anti-APC (1:200; Calbiochem, Ab-1), anti-Flag (1:5000; Sigma, M2), anti-HA (1:5000; Sigma), anti-Myc (1:2000; Calbiochem), anti-Actin (1:5000; Millipore), and rat anti-Flag (1:2000; BioLegend, L5). Signals were quantified by ImageJ.
Cai J., Maitra A., Anders R.A., Taketo M.M, & Pan D. (2015). β-Catenin destruction complex-independent regulation of Hippo–YAP signaling by APC in intestinal tumorigenesis. Genes & Development, 29(14), 1493-1506.
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5

Immunoblotting Protocol Verification

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Immunoblots were carried out as previously described52 (link). Primary antibodies used were: anti-YAP/TAZ (Santa Cruz Biotechnology, sc-101199), anti-P-YAP (Cell Signaling Technology, 4911), anti-LATS (Cell Signaling Technology, 3477), anti-p-LATS (Cell Signaling Technology, 8654) and anti-GAPDH (Millipore, MAB374). Uncropped immunoblots are presented in Supplementary Figure 1.
Panciera T., Citron A., Di Biagio D., Battilana G., Gandin A., Giulitti S., Forcato M., Bicciato S., Panzetta V., Fusco S., Azzolin L., Totaro A., Dei Tos A.P., Fassan M., Vindigni V., Bassetto F., Rosato A., Brusatin G., Cordenonsi M, & Piccolo S. (2020). Reprogramming normal cells into tumor precursors requires ECM stiffness and oncogene-mediated changes of cell mechanical properties. Nature materials, 19(7), 797-806.
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6

Drosophila Western Blot Antibody Protocol

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Antibodies used for Drosophila western blot analysis were: anti-pJNK; anti-pAKT; anti-pMOB; anti-pEGFR; anti-pMEK; anti-pLATS; anti-pGSK3 β -(Cell Signaling); anti-pERK -(Sigma); anti-Actin; anti-Syntaxin; anti-ß-tubulin -(Developmental Studies Hybridoma Bank). Except anti-Syntaxin, all other antibodies were developed against human protein and various previous studies, by our group as well as others, have shown they cross react and can identify the Drosophila protein.
Das T.K., Gatto J.A., Mirmira R., Hourizadeh E., Kaufman D.S., Gelb B.D., & Cagan R. (2020). Drosophila RASopathy Models Identify Disease Subtype Differences and Biomarkers of Drug Efficacy.
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