Carm1

Manufactured by Fortis Life Sciences

CARM1 is a laboratory equipment product designed for use in biomedical research. It functions as a protein arginine methyltransferase, which catalyzes the methylation of arginine residues in target proteins. The core function of CARM1 is to facilitate the study of protein methylation and its role in various biological processes.

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Lab products found in correlation

Senescence β galactosidase kit, by Cell Signaling Technology (1 mentions) H3r17me2a, by Merck Group (1 mentions) β actin, by Merck Group (1 mentions) Dynabeads 280 streptavidin, by Thermo Fisher Scientific (1 mentions) β actin antibody, by Merck Group (1 mentions) Tubulin, by Merck Group (1 mentions) Eif4a3, by Abcam (1 mentions) Gadd45a, by Santa Cruz Biotechnology (1 mentions) Asparagine synthetase, by Santa Cruz Biotechnology (1 mentions) Magoh, by Abcam (1 mentions) Gapdh, by Fortrea (1 mentions) β actin, by Santa Cruz Biotechnology (1 mentions)

4 protocols using carm1

CARM1 Regulation in Bone Marrow and Spleen

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Hematoxylin and Eosin (H&E) staining of fixed bone marrow and spleen tissue was conducted using 6-week-old CARM1^Fl/Fl and CARM1^∆/∆ mice. Antibodies used for analysis of CARM1 and H3R17me2a in 6-week-old mice were CARM1 (Bethyl labs #A300–420A) and Asymmetric-dimethyl H3R17(Abcam #ab8284), respectively. Senescence staining was conducted using the Senescence β - galactosidase kit (Cell Signaling, #9860). Briefly, cytospins containing 2×10⁵ SKNO-1 cells were incubated with staining solution for 36 hr at 37 degrees in a dry incubator prior to imaging.

Greenblatt S.M., Man N., Hamard P.J., Asai T., Karl D., Martinez C., Bilbao D., Stathais V., McGrew-Jermacowicz A., Duffort S., Tadi M., Blumenthal E., Newman S., Vu L., Xu Y., Liu F., Schurer S.C., McCabe M.T., Kruger R.G., Xu M., Yang F.C., Tenen D., Watts J., Vega F, & Nimer S.D. (2018). CARM1 is essential for myeloid leukemogenesis but dispensable for normal hematopoiesis. Cancer cell, 33(6), 1111-1127.e5.

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Generation and Characterization of ADMA-Targeting Antibodies

Cited 1 time

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D4H5, D6A8 and D10F7 were generated against degenerate peptides containing four asymmetric dimethylarginine (ADMA) residues XXXXRme2aXXRme2aXXXXRme2aXXX Rme2aX by Cell Signaling Technology (CST). D4H5 and D6A8 have been previously described20 (link) and are commercially available as part of an ADMA antibody mixture (CST, Catalog #13522). Anti CAS3 antibodies were custom raised by Bethyl laboratories against a peptide pool comprising amino acids 1-20 and 176-195 of human CAS3. CAS3 is also known asFAM168B or MANI; NM_001009993). Anti-methyl CAS3R87me2a (meCAS3) was generated against the epitope CTAVYPVRme2aSAYPQQSR by Covance. Methyl MED12R1899me2a (meMED12) was custom generated against the epitope TSVYRme2aQQQP by CST. PRMT1 antibody was a gift from Stephane Richard (McGill University). H3R2me2a (Millipore, Catalog #05-808), H3R17me2a (Millipore, Catalog #07-214), H3R8me2a (Active Motif, Catalog #39651), CARM1 (Bethyl, Catalog #A300-421A) and β-actin (Sigma, Catalog #A5316) were obtained commercially.

Gayatri S., Cowles M.W., Vemulapalli V., Cheng D., Sun Z.W, & Bedford M.T. (2016). Using oriented peptide array libraries to evaluate methylarginine-specific antibodies and arginine methyltransferase substrate motifs. Scientific Reports, 6, 28718.

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Histone H3 Peptide Binding Assay

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Biotinylated histone H3(23-42) peptides (unmodified, K27ac, R26me2a, and R26me2a+K27ac) were purchased from JPT Peptides Inc. Biotinylated histone H3(18-35) peptides (unmodified, K27M mutated, and K27M mutation with R26me2a modification) were synthesized at Peptide 2.0 Inc. For each pull-down analysis, 0.25 μg of peptide was immobilized onto 25 μl Dynabeads 280 streptavidin (Life Technology, Inc), followed by addition of 1 mg HeLa nuclear extract and incubated at 4°C for 2 h. After binding, the beads were washed three times with wash buffer BC150 (20 mM Tris–HCl pH 7.9, 10% glycerol, 0.2 mM EDTA, 150 mM KCl) before addition of 2× SDS sample buffer and loading for SDS-PAGE and western blot analysis. The antibodies used for western blot were: H3R26me2a antibody from Millipore; H3R17me2a antibody from Active Motif; ELL, ENL, AF9, CARM1, AFF1 and AFF4 antibodies from Bethyl laboratories; p300, Cyclin T1 and CDK9 antibodies from Santa Cruz biotechnology, Inc; and β-actin antibody from Sigma.

Zhang Z., Nikolai B.C., Gates L.A., Jung S.Y., Siwak E.B., He B., Rice A.P., O’Malley B.W, & Feng Q. (2017). Crosstalk between histone modifications indicates that inhibition of arginine methyltransferase CARM1 activity reverses HIV latency. Nucleic Acids Research, 45(16), 9348-9360.

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Antibody-based Protein Expression Analysis

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The following antibodies were used: CARM1 (A300–421A, Bethyl Laboratories); GAPDH (MMS-580S, Covance); β-Actin (sc-47778, Santa Cruz Biotechnology); Tubulin (T6199, Sigma-Aldrich); UPF1 (07–1014, Millipore); UPF2 (D3B10, Cell Signaling); UPF3b (sc-48800, Santa Cruz Biotechnology); Magoh (Ab10686, Abcam); eIF4A3 (Ab32485, Abcam); RBM8a (NB100–55326, Novus Biologicals); Casc3 (LS-C100827, Lifespan Biosciences); Asparagine Synthetase (sc365809, Santa Cruz Biotechnology); Arc (sc15325, Santa Cruz Biotechnology); GADD45a (sc-796, Santa Cruz Biotechnology). Quantitative analyses were done with the ImageJ software.

Sanchez G., Bondy-Chorney E., Laframboise J., Paris G., Didillon A., Jasmin B.J, & Côté J. (2015). A novel role for CARM1 in promoting nonsense-mediated mRNA decay: potential implications for spinal muscular atrophy. Nucleic Acids Research, 44(6), 2661-2676.

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