Skip to main content

Carm1 Products

Carm1 (Coactivator-associated arginine methyltransferase 1; also PRMT4) is a 60-64 kDa member of the Arg N-methyltransferase family of enzymes. It is ubiquitously expressed, and found in the cytoplasm during mitosis, and in the nucleus during the G1, G2 and S phases of the cell cycle. Carm1 binds to nuclear receptor p160 family coactivators. When bound, it methylates DNA-associated histone H3 arginines, allowing for chromatin remodeling and gene activation. It also plays a role in pre-mRNA splicing through its methylation of splicing factors, and regulates the stability of RNA-binding proteins. Human Carm1 is 608 amino acids (aa) in length. It contains one catalytic site between aa 184-394, and a transactivation domain at the C-terminus (aa 499-608). There is one automethylation site at Arg550, and a phosphorylation site at Ser216 that, when utilized, promotes cytosolic localization. Carm1 likely forms homodimers. There are three potential isoform variants. One shows an alternative start site at Met378, a second possesses a 16 aa substitution for aa 369-608, and a third contains a deletion of aa 539-561. Over aa 209-379, human and mouse Carm1 are identical in aa sequence.

Show More

137 results for "Carm1" in Products

Back to Search Results
Apply

137 results for "Carm1" in Products

Carm1 Products

Carm1 (Coactivator-associated arginine methyltransferase 1; also PRMT4) is a 60-64 kDa member of the Arg N-methyltransferase family of enzymes. It is ubiquitously expressed, and found in the cytoplasm during mitosis, and in the nucleus during the G1, G2 and S phases of the cell cycle. Carm1 binds to nuclear receptor p160 family coactivators. When bound, it methylates DNA-associated histone H3 arginines, allowing for chromatin remodeling and gene activation. It also plays a role in pre-mRNA splicing through its methylation of splicing factors, and regulates the stability of RNA-binding proteins. Human Carm1 is 608 amino acids (aa) in length. It contains one catalytic site between aa 184-394, and a transactivation domain at the C-terminus (aa 499-608). There is one automethylation site at Arg550, and a phosphorylation site at Ser216 that, when utilized, promotes cytosolic localization. Carm1 likely forms homodimers. There are three potential isoform variants. One shows an alternative start site at Met378, a second possesses a 16 aa substitution for aa 369-608, and a third contains a deletion of aa 539-561. Over aa 209-379, human and mouse Carm1 are identical in aa sequence.

Show More
Applications: IHC
Reactivity: Human
Applications: IHC
Reactivity: Human
Applications: IHC
Reactivity: Human
Applications: IHC
Reactivity: Human
Applications: IHC
Reactivity: Human
Applications: IHC
Reactivity: Human
Applications: IHC, WB, ICC/IF, KO
Reactivity: Human
Applications: IHC, WB, IP, KD
Reactivity: Human, Mouse
Applications: WB, ICC, KO
Reactivity: Human, Mouse
Applications: IHC, WB, ELISA, ICC/IF, Flow
Reactivity: Human, Rat, Monkey, Primate
Applications: IHC, WB, IP
Reactivity: Human, Mouse
Applications: IHC, ICC/IF
Reactivity: Human
Applications: IHC, WB
Reactivity: Human
Applications: WB, ELISA, MA, AP
Applications: WB
Reactivity: Human
Applications: WB
Applications: ICC/IF
Reactivity: Human
Applications: ICC/IF
Reactivity: Human
Applications: IHC
Reactivity: Human
Applications: AC
Applications: AC
Applications: AC
Applications: IHC, ICC/IF
Reactivity: Human
Applications: IHC, ICC/IF
Reactivity: Human
Applications: IHC, ICC/IF
Reactivity: Human
Results Per Page
5 10 25 50
/ 6