Anti-PRMT3 Antibody Picoband® Fluoro488 Conjugated

Protein arginine N-methyltransferase 3 is an enzyme that in humans is encoded by the PRMT3 gene. This gene belongs to the protein arginine methyltransferase (PRMT) family. The encoded enzyme catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. The enzyme acts on 40S ribosomal protein S2 (rpS2), which is its major in-vivo substrate, and is involved in the proper maturation of the 80S ribosome. Alternative splicing results in multiple transcript variants.

N-alpha-acetyltransferase 15, NatA auxiliary subunit; Gastric cancer antigen Ga19; N-terminal acetyltransferase; NMDA receptor-regulated protein 1; Protein tubedown-1; Tbdn100; NAA15; GA19, NARG1, NATH, TBDN100

Expressed at high levels in testis and in ocular endothelial cells. Also found in brain (corpus callosum), heart, colon, bone marrow and at lower levels in most adult tissues, including thyroid, liver, pancreas, mammary and salivary glands, lung, ovary, urogenital system and upper gastrointestinal tract. Overexpressed in gastric cancer, in papillary thyroid carcinomas and in a Burkitt lymphoma cell line (Daudi) . Specifically suppressed in abnormal proliferating blood vessels in eyes of patients with proliferative diabetic retinopathy. .

Cancer, Cancer Susceptibility, Cardiovascular, Domain Families, Epigenetics and Nuclear Signaling, Hlh/Leucine Zipper, Hypertrophy, Immunology, Innate Immunity, Oncoproteins, Oncoproteins/Suppressors, Proto-Oncogenes, TLR Signaling, Transcription, Transcription Factors

Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. .

1. Tang, J., Gary, J. D., Clarke, S., Herschman, H. R. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J. Biol. Chem. 273: 16935-16945, 1998. 2. Wolf, S. S. The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans. Cell. Molec. Life Sci. 66: 2109-2121, 2009.

Cytoplasm. Nucleus. Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton-bound polysomes, but not in the membrane-bound polysomes.