You are viewing an incomplete version of our website. Please click to reload the website as full version.

Coactivator-Associated Arginine Methyltransferase 1 (CARM1) (AA 45-69), (AA 595-608) antibody

Details for Product No. ABIN123415, Supplier: Login to see New
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

AA 45-69, AA 595-608
(26), (25), (21), (16), (15), (13), (7), (5), (4), (3), (3), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1)
(181), (76), (75), (6), (1), (1)
(164), (16), (2), (1)
(9), (9), (9), (6), (6), (6), (3), (3), (3), (3), (3), (3), (3), (3), (3)
Western Blotting (WB)
(142), (69), (41), (33), (31), (24), (18), (10), (7), (2)
Pubmed 5 references available
Supplier Login to see New
Catalog number from supplier Login to see New
Quantity 0.1 mg
Shipping to United States ( )
Immunogen Synthetic peptides containing amino acids 45-69 and 595-608 of human PRMT4
Purification Protein G chromatography
Alternative Name CARM1 / PRMT4 (CARM1 Antibody Abstract)
Background Protein arginine methylation is an important posttranslational modification in eukaryotic cells, which has been implicated in RNA processing and trafficking, receptor-mediated signaling, and transcription. CARM1 (coactivator-associated arginine methyltransferase-1) also known as PRMT4 (protein-arginine N-methyltransferase-4) belongs to a family of proteins that catalyzes the methylation of arginine residues. The PRMT proteins are recruited by C-terminal activation domain-2 of the SRC (steroid receptor coactivator) GRIP-1, whereas p300 interacts with activation domain-1 in the C terminus. CARM1 can methylate histone H3 in vitro, and a mutation in the putative S-adenosylmethionine binding domain of CARM1 substantially reduces both methyltransferase and coactivator activities suggesting that coactivator-mediated methylation of proteins in the transcription machinery may contribute to transcriptional regulation. Alternate Names: Histone-Arginine Methyltransferase CARM1, Protein Arginine N-Methyltransferase 4, EC=, EC=2.1.1.-, CARM-1, Coactivator-Associated Arginine Methyltransferase 1.
UniProt Q86X55
Application Notes Western blot: 0.5 - 2.0 ug/ml. Recommended positive control: HeLa cell lysate. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/mL
Buffer PBS, containing 0.05% sodium azide and 0.05 % BSA
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Store the antibody at 2-8°C for one month or at -20°C for longer. Avoid repeated freezing and thawing. Shelf Life: one year from despatch.
Expiry Date 12 months
Supplier Images
Western Blotting (WB) image for anti-Coactivator-Associated Arginine Methyltransferase 1 (CARM1) (AA 45-69), (AA 595-608) antibody (ABIN123415) Western blot analysis of PRMT4 in cell lysates from HeLa cells using ABIN123415 at 0....
General Chen, Loffler, Chen et al.: "The coactivator-associated arginine methyltransferase is necessary for muscle differentiation: CARM1 coactivates myocyte enhancer factor-2." in: The Journal of biological chemistry, Vol. 277, Issue 6, pp. 4324-33, 2002 (PubMed).

Koh, Chen, Lee et al.: "Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities." in: The Journal of biological chemistry, Vol. 276, Issue 2, pp. 1089-98, 2001 (PubMed).

Chen, Huang, Stallcup: "Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300." in: The Journal of biological chemistry, Vol. 275, Issue 52, pp. 40810-6, 2001 (PubMed).

Chen, Ma, Hong et al.: "Regulation of transcription by a protein methyltransferase." in: Science (New York, N.Y.), Vol. 284, Issue 5423, pp. 2174-7, 1999 (PubMed).

Smith, Ruecknagel, Schierhorn et al.: "Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3." in: The Journal of biological chemistry, Vol. 274, Issue 19, pp. 13229-34, 1999 (PubMed).

Catalog No. ABIN123415

Order hotline:

  • +1 877 302 8632
  • +1 888 205 9894 (TF)