Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

PRMT1 (F339) Antibody #2453

methyltransferase   PRMT  

No. Size Price
2453S 100 µl ( 10 western blots ) ¥3,250.00 现货查询 购买询价 防伪查询
2453 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat,Monkey, Endogenous 41 Rabbit

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,


Species predicted to react based on 100% sequence homology: Bovine,

Specificity / Sensitivity

PRMT1 (F339) Antibody detects endogenous levels of total PRMT1 protein (all three isoforms). The antibody does not cross-react with other PRMT proteins.

PRMT1 (F339) Antibody能够检测内源性PRMT1的总蛋白水平(所有三个亚型)。该抗体不能与其它PRMT蛋白发生相互作用。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of human PRMT1. Antibodies are purified by protein A and peptide affinity chromatography.


Western Blotting

Western Blotting

Western blot analysis of cell lysates from A549, NIH/3T3, H-4-II-E and COS cells using PRMT1 Antibody.

使用PRMT1 Antibody,免疫印迹(Western blot)分析A549、NIH/3T3、H-4-II-E和COS细胞中PRMT1的蛋白水平。


Protein arginine N-methyltransferase 1 (PRMT1) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). Though all PRMT proteins catalyze the formation of mono-methyl arginine, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce an asymmetric di-methyl arginine while Type II PRMTs (PRMT 5 and 7) produce symmetric di-methyl arginine (1). Mono-methyl arginine, but not di-methyl arginine, can be converted to citrulline through deimination catalyzed by enzymes such as PADI4 (2). Most PRMTs, including PRMT1, methylate arginine residues found within glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (1). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3). PRMT1 methylates Arg3 of histone H4 and cooperates synergistically with p300/CBP to enhance transcriptional activation by nuclear receptor proteins (4-6). In addition, PRMT1 methylates many non-histone proteins, including the orphan nuclear receptor HNF4 (6), components of the heterogeneous nuclear ribonucleoprotein (hnRNP) particle (7), the RNA binding protein Sam68 (8), interleukin enhancer-binding factor 3 (ILF3) (9) and interferon-α and β receptors (10). These interactions suggest additional functions in transcriptional regulation, mRNA processing and signal transduction. Alternative mRNA splicing produces three enzymatically active PMRT1 isoforms that differ in their amino-terminal regions (11). PRMT1 is localized to the nucleus or cytoplasm, depending on cell type (12,13) and appears in many distinct protein complexes. ILF3, TIS21 and the leukemia-associated BTG1 proteins bind PRMT1 to regulate its methyltransferase activity (9,14).

Protein arginine N-methyltransferase 1 (PRMT1)是蛋白质精氨酸甲基转移酶(PRMT)蛋白家族的一个成员,它以S-腺苷-甲硫氨酸(S-adenosylmethionine,AdoMet)为甲基供体,把甲基转移到蛋白质精氨酸胍基的氮原子上 (1)。虽然所有PRMT蛋白催化单甲基精氨酸的形成,I 型PRMTs (PRMT1, 3, 4, and 6)增加一个附加的甲基能产生一个不对称双甲基精氨酸,然而II型PRMTs (PRMT 5 and 7)产生对称型双甲基精氨酸(1)。单甲基精氨酸而不是双甲基精氨酸,它能通过由酶例如PADI4催化deimination过程去转换成瓜氨酸(2)。许多PRMTs包括PRMT1,在甘氨酸 - 精氨酸富足(GAR)蛋白区域,例如RGG, RG, and RXR重复序列中发现甲基化精氨酸残基(1)。然而,PRMT4/CARM1 and PRMT5可以使PGM (proline-, glycine-, methionine-rich) 结构中精氨酸甲基化(3)。PRMT1能够使组蛋白H4的Arg3位点甲基化,并且通过细胞核受体蛋白与p300/CBP协同调节去提高转录激活(4-6)。此外,PRMT1可以使许多非组蛋白甲基化,包括孤儿核受体(orphan nuclear receptor)HNF4 (6)、核不均一性核糖核蛋白(heterogeneous nuclear ribonucleoprotein, hnRNP)(7)、RNA结合蛋白Sam68 (8)、白介素增强结合因子3(ILF3) (9)和interferon-α and β受体(10)。这些相互作用认为另外的功能是转录调控、mRNA加工和信号转导。mRNA选择性剪切能产生三种具有酶促活性PMRT1亚型,它们在氨基端区域存在差异(11)。PRMT1是定位于细胞核或细胞质,这取决于细胞形态(12,13)以及在许多明显的蛋白复合物中出现。ILF3、TIS21和白介素相关的BTG1蛋白能结合PRMT1去调节它的甲基转移酶活性(9,14)。

  1. Bedford, M.T. and Richard, S. (2005) Mol. Cell 18, 263-272.
  2. Wang, Y. et al. (2004) Science 306, 279-283.
  3. Cheng, D. et al. (2007) Mol. Cell 25, 71-83.
  4. Wang, H. et al. (2001) Science 293, 853-857.
  5. Strahl, B.D. et al. (2001) Curr. Biol. 11, 996-1000.
  6. Barrero, M.J. and Malik, S. (2006) Mol. Cell 24, 233-243.
  7. Nichols, R.C. et al. (2000) Exp. Cell Res. 256, 522-532.
  8. Côté, J. et al. (2003) Mol. Biol. Cell 14, 274-287.
  9. Tang, J. et al. (2000) J. Biol. Chem. 275, 19866-19876.
  10. Abramovich, C. et al. (1997) EMBO J. 16, 260-266.
  11. Scorilas, A. et al. (2000) Biochem. Biophys. Res. Commun. 278, 349-359.
  12. Frankel, A. et al. (2002) J. Biol. Chem. 277, 3537-3543.
  13. Herrmann, F. et al. (2005) J. Biol. Chem. 280, 38005-38010.
  14. Lin, W.J. et al. (1996) J. Biol. Chem. 271, 15034-15044.

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