Immunogen | E. coli-derived recombinant human Carm1 Lys209-Leu379 Accession # Q86X55 |
Specificity | Detects human Carm1 in direct ELISAs and Western blots. |
Source | N/A |
Isotype | IgG |
Clonality | Polyclonal |
Host | Goat |
Gene | CARM1 |
Purity Statement | Antigen Affinity-purified |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Dilutions |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Preservative | No Preservative |
Concentration | LYOPH |
Reconstitution Instructions | Sterile PBS to a final concentration of 0.2 mg/mL. |
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.
Secondary Antibodies |
Isotype Controls |
Epigenetic Control of Autophagy By Christina Towers, PhD. In the last 20 years, epigenetic regulation has become front and center for almost all fields of biology and its role in diseases like cancer and neurodegeneration are being heavily studi... Read full blog post. |
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