Anti-PRMT7 Antibody Picoband® fluoro488 Vervoeging

Protein arginine methyltransferase 7 is a protein that in humans is encoded by the PRMT7 gene. This gene encodes a member of the protein arginine N-methyltransferase family of proteins. The encoded enzyme transfers single methyl groups to arginine residues to generate monomethylarginines on histone proteins as well as other protein substrates. This enzyme plays a role in a wide range of biological processes, including neuronal differentiation, male germ line imprinting, small nuclear ribonucleoprotein biogenesis, and regulation of the Wnt signaling pathway. Mutations in this gene underlie multiple related syndromes in human patients characterized by intellectual disability, short stature and other features. The encoded protein may promote breast cancer cell invasion and metastasis in human patients.

Serine protease HTRA3;3.4.21.-; High-temperature requirement factor A3; Pregnancy-related serine protease; HTRA3; PRSP

PRMT7

54496

Q9NVM4

Human, Mouse, Rat

No cross-reactivity with other proteins.

E.coli-derived human PRMT7 recombinant protein (Position: K121-D526) .

Widely expressed, with highest levels in both adult and fetal heart, ovary, uterus placenta, and bladder. In the endometrium, expressed in epithelial glands and the stroma. Also present in leukocytes. Isoform 1 is predominant in heart and skeletal muscle, whereas isoform 2 is predominant in placenta and kidney. .

Flow Cytometry

Alzheimer's Disease, Cell Biology, Metalloprotease, Neurodegenerative Disease, Neurology Process, Neuroscience, Proteolysis/Ubiquitin, Proteolytic Enzymes, Sensory System, Visual System

Immunogen affinity purified.

Liquid

Serine protease that cleaves beta-casein/CSN2 as well as several extracellular matrix (ECM) proteoglycans such as decorin/DCN, biglycan/BGN and fibronectin/FN1. Inhibits signaling mediated by TGF-beta family proteins possibly inly by degradation of these ECM proteoglycans (By similarity) . May act as a tumor suppressor. Negatively regulates, in vitro, trophoblast invasion during placental development and may be involved in the development of the placenta in vivo. May also have a role in ovarian development, granulosa cell differentiation and luteinization (PubMed:21321049, PubMed:22229724) . .

1. Akawi, N., McRae, J., Ansari, M., Balasubramanian, M., Blyth, M., Brady, A. F., Clayton, S., Cole, T., Deshpande, C., Fitzgerald, T. W., Foulds, N., Francis, R., and 30 others. Discovery of four recessive developmental disorders using probabilistic genotype and phenotype matching among 4,125 families. Nature Genet. 47: 1363-1369, 2015. 2. Birnbaum, R., Yosha-Orpaz, N., Yanoov-Sharav, M., Kidron, D., Gur, H., Yosovich, K., Lerman-Sagie, T., Malinger, G. Prenatal and postnatal presentation of PRMT7 related syndrome: expanding the phenotypic manifestations. Am. J. Med. Genet. 179A: 78-84, 2019. 3. Kernohan, K. D., McBride, A., Xi, Y., Martin, N., Schwartzentruber, J., Dyment, D. A., Majewski, J., Blaser, S. Care4Rare Canada Consortium, Boycott, K. M., Chitayat, D. Loss of the arginine methyltranserase (sic) PRMT7 causes syndromic intellectual disability with microcephaly and brachydactyly. Clin. Genet. 91: 708-716, 2017.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

48608 MW

6

Serine protease HTRA3

Secreted . Secretion increased during decidualization of endometrial stromal cells.

Serine protease HTRA3

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.