Anti suv39h1

Manufactured by Abcam

Sourced in United Kingdom, Hong Kong

Anti-SUV39H1 is a primary antibody that targets the SUV39H1 protein. SUV39H1 is a histone methyltransferase that is involved in the regulation of gene expression and chromatin structure.

Automatically generated - may contain errors

Lab products found in correlation

Spelling variants of this product

Anti-SUV39H1 antibody (4 citations) Suv39h1 (3 citations)

4 protocols using anti suv39h1

Epigenetic Regulation in EMT Signaling

Check if the same lab product or an alternative is used in the 5 most similar protocols

PVDF membrane was obtained from Millipore (Bedford, MA, USA); anti-E-cadherin, anti-N-cadherin, anti-SET7/9, anti-OGG1/2, anti-HDAC3, LSD1 shRNA plasmid and JMJD2a shRNA plasmid were obtained from Santa Cruz Biotechnology (Santa Cruz, CA, USA); anti-FLAG and anti-smooth muscle actin antibody and Phalloidin-TRITC were obtained from Sigma-Aldrich (St Louis, MO, USA); DCFDA and Alexa 488 secondary antibody were obtained from Molecular Probes; anti-H3K4me2, anti-H3K4me3, anti-H3K9me2, anti-H3K9me3, anti-H3, anti-LSD1, anti-JMJD2A, anti-SUV39H1, anti-NCoR1, anti-APE1, anti-β-actin, anti-β-tubulin antibodies, anti-IgG mouse and anti-IgG rabbit were obtained from Abcam (Cambridge, UK); anti-pSMAD2/3 (Ser 423/425) and anti-SMAD2/3 antibodies were obtained from Cell Signaling Technology (Danvers, MA, USA); anti-8-oxo-dG antibodies were obtained from Trevigen Inc. (Gaithersburg, MD, USA); and the OxyDNA assay was obtained from Calbiochem (San Diego, CA, USA).

Pezone A., Taddei M.L., Tramontano A., Dolcini J., Boffo F.L., De Rosa M., Parri M., Stinziani S., Comito G., Porcellini A., Raugei G., Gackowski D., Zarakowska E., Olinski R., Gabrielli A., Chiarugi P, & Avvedimento E.V. (2020). Targeted DNA oxidation by LSD1–SMAD2/3 primes TGF-β1/ EMT genes for activation or repression. Nucleic Acids Research, 48(16), 8943-8958.

+ Open protocol

+ Expand

Quantitative Western Blot Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols

Cells protein lysates were separated by 10% sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) transferred to 0.22 μm NC membranes (Sigma) and incubated with specific antibodies. Autoradiograms were quantified by densitometry (Quantity One software; Bio-Rad). β-actin antibody was used as control. Anti-EZH2, Anti-SUV39H1, Anti-SPRY4 and Anti-HOXB13 was from Abcam (Hong Kong, China).

Zhang E., Han L., Yin D., He X., Hong L., Si X., Qiu M., Xu T., De W., Xu L., Shu Y, & Chen J. (2016). H3K27 acetylation activated-long non-coding RNA CCAT1 affects cell proliferation and migration by regulating SPRY4 and HOXB13 expression in esophageal squamous cell carcinoma. Nucleic Acids Research, 45(6), 3086-3101.

+ Open protocol

+ Expand

Chromatin Immunoprecipitation (ChIP) Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols

ChIP assays were performed according to previously described Protocols [28 (link)]. In brief, ChIP was performed using the EZ-Magna ChIP Chromatin Immunoprecipitation Kit (Millipore). The antibodies were obtained from Abcam: anti-H3K9 (ab8898) and anti-SUV39H1 (Abcam, ab12405). The DNA was detected through RT-qPCR and primers were provided in Additional file 2: Table S2.

Bian E., Chen X., Xu Y., Ji X., Cheng M., Wang H., Fang Z, & Zhao B. (2019). A central role for MeCP2 in the epigenetic repression of miR-200c during epithelial-to-mesenchymal transition of glioma. Journal of Experimental & Clinical Cancer Research : CR, 38, 366.

+ Open protocol

+ Expand

ChIP-qPCR for Epigenetic Markers

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Chromatin immunoprecipitation was performed as previously described [40 (link)]. Briefly, the cells were incubated with 1% formaldehyde for cross-linking, followed by shearing. The chromatin solution was obtained by centrifugation at 13,000 rpm at 4 °C rpm for 20 min. A small portion (5%) of the chromatin solution was reserved as input DNA, and the remaining solution was incubated with the primary antibodies and protein A agarose/salmon sperm (Millipore, #16-157) overnight at 4 °C. Next, the chromatin fragments were de-crossed from the proteins and eluted to be subjected to qPCR using primers listed in Table 2. Anti-HP1γ (Millipore, 05-690), anti-trimethyl Histone H3 Lys9 (Millipore, 07-442), anti-G9a (Abcam, ab40542), and anti-Suv39h1 (Abcam, ab12405) were used for ChIP.

Yi S.A., Kim G.W., Yoo J., Han J.W, & Kwon S.H. (2020). HP1γ Sensitizes Cervical Cancer Cells to Cisplatin through the Suppression of UBE2L3. International Journal of Molecular Sciences, 21(17), 5976.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!