CARM1 sirna

CARM1 siRNA (Mouse)

Cat. Num. AAA8230859

• Gene Names: Carm1; Prmt4
• Reactivity: Mouse
• Applications: RNA Interference (RNAi)
• Purity: > 97%
• Synonyms: CARM1; CARM1 siRNA (Mouse); PRMT4; Histone-arginine methyltransferase CARM1; Coactivator-associated arginine methyltransferase 1; Protein arginine N-methyltransferase 4; CARM1 sirna

• Host: Synthetic
• Reactivity: Mouse
• Specificity: CARM1 siRNA (Mouse) is a target-specific 19-23 nt siRNA oligo duplexes designed to knock down gene expression.
• Purity/Purification: > 97%
• Form/Format: Lyophilized powder
• Sequence Length: 585

• Applicable Applications for CARM1 sirna: RNA Interference (RNAi)
• Quality Control: Oligonucleotide synthesis is monitored base by base through trityl analysis to ensure appropriate coupling efficiency. The oligo is subsequently purified by affinity-solid phase extraction. The annealed RNA duplex is further analyzed by mass spectrometry to verify the exact composition of the duplex. Each lot is compared to the previous lot by mass spectrometry to ensure maximum lot-to-lot consistency.
• Directions for Use: We recommends transfection with 100 nM siRNA 48 to 72 hours prior to cell lysis. Before resuspending, briefly centrifuge the tube to ensure the lyophilized siRNA is at the bottom of the tube. Resuspend the siRNA oligos to an appropriate concentration with DEPC water. For each vial, suitable for 250 transfections in 24 well plate (20 pmol for each well).
• Components: We offer pre-designed sets of 3 different target-specific siRNA oligo duplexes of mouse CARM1 gene. Each vial contains 5 nmol of lyophilized siRNA. The duplexes can be transfected individually or pooled together to achieve knockdown of the target gene, which is most commonly assessed by qPCR or western blot. Our siRNA oligos are also chemically modified (2'-OMe) at no extra charge for increased stability and enhanced knockdown in vitro and in vivo.
• Preparation and Storage: Shipped at 4 degree C. Store at -20 degree C for one year.

Related Product Information for CARM1 sirna

siRNA to inhibit CARM1 expression using RNA interference

NCBI and Uniprot Product Information

• NCBI GI #: 50511310
• NCBI GeneID: 59035
• NCBI Accession #: NP_067506.2
• NCBI GenBank Nucleotide #: NM_021531.6
• UniProt Accession #: Q9WVG6; Q3TYB9; Q8K1Y5; Q91W24; Q99KX8
• Molecular Weight: 63,460 Da
• NCBI Official Full Name: histone-arginine methyltransferase CARM1 isoform 1
• NCBI Official Synonym Full Names: coactivator-associated arginine methyltransferase 1
• NCBI Official Symbol: Carm1
• NCBI Official Synonym Symbols: Prmt4
• NCBI Protein Information: histone-arginine methyltransferase CARM1
• UniProt Protein Name: Histone-arginine methyltransferase CARM1
• Protein Family: Histone-arginine methyltransferase
• UniProt Gene Name: Carm1
• UniProt Synonym Gene Names: Prmt4
• UniProt Entry Name: CARM1_MOUSE

Uniprot Description

CARM1: a protein arginine methyltransferase that methylates histones and other proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginine residues. A key epigenetic regulator of hematopoiesis affecting multiple lineages. Recruited to promoters upon gene activation together with histone acetyltransferases from P300 and p160 families, methylates histone H3 at R17 (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2 activation, acts synergically with P300 and either one of the p160 histone acetyltransferases SRC1, NCoA2 and SRC-3 or CTNNB1 to activate transcription. During myogenic transcriptional activation, acts together with SRC-3 as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53 transcriptional activation. Methylates P300, both at R 2142, which may loosen its interaction with NCoA2, and at R580 and R604 in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Methylates RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA- stabilizing properties and the half-life of their target mRNAs. Interacts with the C-terminus of NCoA2, SRC-3 and SRC1. Part of a complex consisting of CARM1, P300 and NCoA2. Interacts with FLII, TP53, myogenic factor MEF2, P300, TRIM24, CREBBP and CTNNB1. Identified in a complex containing CARM1, TRIM24 and NCoA2. Interacts with SRC3. Interacts with SNRPC. Interacts with NR1H4. Interacts with RELA. Interacts with HTLV-1 Tax-1. Overexpressed in prostate adenocarcinomas and high-grade prostatic intraepithelial neoplasia. Methylation of H3R17 (H3R17me) by CARM1 is stimulated by preacetylation of H3 K18 (H3K18ac) H3 K23 (H3K23ac) by EP300 and blocked by citrullination of H3 R17 (H3R17ci) by PADI4. Belongs to the protein arginine N-methyltransferase family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Methyltransferase, protein arginine; EC 2.1.1.125; Methyltransferase; Nuclear receptor co-regulator

Cellular Component: nucleoplasm; cytoplasm; cytosol; nucleus

Molecular Function: methyltransferase activity; protein homodimerization activity; trimethylamine methyltransferase activity; monomethylamine methyltransferase activity; RNA methyltransferase activity; tRNA (cytosine)-methyltransferase activity; rRNA (cytosine-C5-967)-methyltransferase activity; rRNA (uridine) methyltransferase activity; N-methyltransferase activity; tRNA (guanine) methyltransferase activity; rRNA (adenine-N6,N6-)-dimethyltransferase activity; arginine N-methyltransferase activity; selenocysteine methyltransferase activity; methanol-specific methylcobalamin:coenzyme M methyltransferase activity; protein-arginine N-methyltransferase activity; tRNA (guanine-N2-)-methyltransferase activity; dimethylamine methyltransferase activity; protein methyltransferase activity; 2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; transferase activity; hydroxyneurosporene-O-methyltransferase activity; rRNA (uridine-2'-O-)-methyltransferase activity; tRNA (uracil) methyltransferase activity; rRNA (adenine) methyltransferase activity; C-methyltransferase activity; cobalt-precorrin-6B C5-methyltransferase activity; cobalt-precorrin-3 C17-methyltransferase activity; 1-phenanthrol methyltransferase activity; transcription coactivator activity; S-methyltransferase activity; lysine N-methyltransferase activity; DNA-methyltransferase activity; tRNA (cytosine-5-)-methyltransferase activity; tRNA (adenine)-methyltransferase activity; C-terminal protein carboxyl methyltransferase activity; rRNA (cytosine) methyltransferase activity; cobalt-precorrin-7 C15-methyltransferase activity; protein-arginine N5-methyltransferase activity; rRNA methyltransferase activity; histone methyltransferase activity; protein-arginine omega-N asymmetric methyltransferase activity; histone-arginine N-methyltransferase activity; protein-leucine O-methyltransferase activity; demethylmenaquinone methyltransferase activity; rRNA (adenine-N6-)-methyltransferase activity; tRNA methyltransferase activity; rRNA (guanine) methyltransferase activity; methylarsonite methyltransferase activity; protein binding; mRNA methyltransferase activity; methylamine-specific methylcobalamin:coenzyme M methyltransferase activity; ligand-dependent nuclear receptor transcription coactivator activity; tRNA (guanine-N1-)-methyltransferase activity; cobalt-precorrin-5B C1-methyltransferase activity; protein-lysine N-methyltransferase activity; O-methyltransferase activity; tRNA (adenine-N1-)-methyltransferase activity; tRNA (adenine-57, 58-N(1)-) methyltransferase activity

Biological Process: methylation; steroid hormone receptor signaling pathway; regulation of estrogen receptor signaling pathway; estrogen receptor signaling pathway; response to cAMP; transcription, DNA-dependent; protein amino acid methylation; pathogenesis; chromatin modification; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; histone methylation; regulation of transcription, DNA-dependent; positive regulation of cell proliferation; positive regulation of fat cell differentiation; negative regulation of protein binding