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Tri methyl histone h3 lys27 polyclonal

Manufactured by Cell Signaling Technology
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Tri-Methyl-Histone H3(Lys27) polyclonal is a lab equipment product that detects the tri-methylation of lysine 27 on histone H3. This modification is associated with gene silencing and repression of transcription.

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Lab products found in correlation

Total polyclonal, by Cell Signaling Technology (2 mentions) β actin clone a5441, by Merck Group (2 mentions) Collagen 1 clone col 1, by Abcam (2 mentions) Tead1 clone 610923, by BD (2 mentions) Ezh2 polyclonal, by BD (2 mentions) Total histone h3 polyclonal, by Cell Signaling Technology (2 mentions) Phospho smad3 polyclonal, by Cell Signaling Technology (2 mentions) Pu 1 polyclonal, by Cell Signaling Technology (2 mentions) Hrp conjugated secondary antibody, by Agilent Technologies (2 mentions) Bradford protein assay, by Bio-Rad (2 mentions)

Spelling variants of this product

Histone H3 (504 citations) Tri-Methyl-Histone H3 (Lys27) (12 citations) Tri-Methyl-Histone H3 (7 citations)

2 protocols using tri methyl histone h3 lys27 polyclonal

1

Quantitative Protein Expression Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein concentrations were determined using the Bradford Protein Assay according to the manufacturer’s protocol (Bio-Rad). Same amounts of protein were loaded on a Tris-Glycine buffered gel. Proteins were separated by SDS-PAGE and transferred to PVDF membrane. The membrane was incubated with the appropriate primary antibody and HRP-conjugated secondary antibodies (Dako, Glostrup, Denmark). The following antibodies were used: β-Actin clone A5441 (1/10000, Sigma-Aldrich), Collagen I clone COL-1 (1/1000, abcam), TEAD1 clone 610923 (1/500, BD Biosciences), EZH2 polyclonal (4905, 1/2000), total histone H3 polyclonal (9715, 1/1000), Tri-Methyl-Histone H3(Lys27) polyclonal (9733, 1/1000), total polyclonal (9513, 1/1000) or phospho-Smad3 polyclonal (9520, 1/1000) and PU.1 polyclonal (2266, 1/500) (all Cell Signaling). As secondary antibodies in western blot anti-mouse polyclonal (P0447, 1/1500) or anti-rabbit polyclonal (P0448, 1/2000) HRP-conjugated secondary antibodies (all Dako) were used. Blots were visualized using enhanced chemiluminescence (ECL). β-Actin was used as a loading control. Western Blots were quantified using ImageJ Software (version 1.46r).
Wohlfahrt T., Rauber S., Uebe S., Luber M., Soare A., Ekici A., Weber S., Matei A.E., Chen C.W., Maier C., Karouzakis E., Kiener H.P., Pachera E., Dees C., Beyer C., Daniel C., Gelse K., Kremer A.E., Naschberger E., Stürzl M., Butter F., Sticherling M., Finotto S., Kreuter A., Kaplan M.H., Jüngel A., Gay S., Nutt S.L., Boykin D.W., Poon G.M., Distler O., Schett G., Distler J.H, & Ramming A. (2019). SPI1/PU.1 controls fibroblast polarization and tissue fibrosis. Nature, 566(7744), 344-349.
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2

Quantitative Protein Expression Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein concentrations were determined using the Bradford Protein Assay according to the manufacturer’s protocol (Bio-Rad). Same amounts of protein were loaded on a Tris-Glycine buffered gel. Proteins were separated by SDS-PAGE and transferred to PVDF membrane. The membrane was incubated with the appropriate primary antibody and HRP-conjugated secondary antibodies (Dako, Glostrup, Denmark). The following antibodies were used: β-Actin clone A5441 (1/10000, Sigma-Aldrich), Collagen I clone COL-1 (1/1000, abcam), TEAD1 clone 610923 (1/500, BD Biosciences), EZH2 polyclonal (4905, 1/2000), total histone H3 polyclonal (9715, 1/1000), Tri-Methyl-Histone H3(Lys27) polyclonal (9733, 1/1000), total polyclonal (9513, 1/1000) or phospho-Smad3 polyclonal (9520, 1/1000) and PU.1 polyclonal (2266, 1/500) (all Cell Signaling). As secondary antibodies in western blot anti-mouse polyclonal (P0447, 1/1500) or anti-rabbit polyclonal (P0448, 1/2000) HRP-conjugated secondary antibodies (all Dako) were used. Blots were visualized using enhanced chemiluminescence (ECL). β-Actin was used as a loading control. Western Blots were quantified using ImageJ Software (version 1.46r).
Wohlfahrt T., Rauber S., Uebe S., Luber M., Soare A., Ekici A., Weber S., Matei A.E., Chen C.W., Maier C., Karouzakis E., Kiener H.P., Pachera E., Dees C., Beyer C., Daniel C., Gelse K., Kremer A.E., Naschberger E., Stürzl M., Butter F., Sticherling M., Finotto S., Kreuter A., Kaplan M.H., Jüngel A., Gay S., Nutt S.L., Boykin D.W., Poon G.M., Distler O., Schett G., Distler J.H, & Ramming A. (2019). SPI1/PU.1 controls fibroblast polarization and tissue fibrosis. Nature, 566(7744), 344-349.
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