PRMT5 Antibodies

Protein arginine N-methyltransferase 5 (PRMT5)

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:10531356, PubMed:11152681, PubMed:11747828, PubMed:12411503, PubMed:15737618, PubMed:17709427, PubMed:20159986, PubMed:20810653, PubMed:21258366, PubMed:21917714, PubMed:22269951, PubMed:21081503). Especially mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); these methylation being required for the assembly and biogenesis of snRNP core particles (PubMed:12411503, PubMed:11747828, PubMed:17709427).

Methylates SUPT5H and might regulate its transcriptional elongation properties (PubMed:12718890). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro.

Gene Information

Human
Gene Name:	PRMT5
Uniprot:	O14744
Entrez:	10419

Family

Belongs to:
class I-like SAM-binding methyltransferase superfamily

Alternative Names

EC 2.1.1.-; EC 2.1.1.125; Histone-arginine N-methyltransferase PRMT5; HMT1 hnRNP methyltransferase-like 5,72 kDa ICln-binding protein; HRMT1L5; IBP72; Jak-binding protein 1; JBP1; protein arginine methyltransferase 5; protein arginine N-methyltransferase 5; Shk1 kinase-binding protein 1 homolog; skb1 (S. pombe) homolog; SKB1 homolog (S. pombe); SKB1; SKB1HsSKB1 homolog

Molecular Weight

Mass (kDA):
72.684 kDA

Genomic Context

Human
Location:	14q11.2
Sequence:	14; NC_000014.9 (22920526..22929392, complement)

Tissue Specificity

Ubiquitous.

Subcellular Localizations

Cytoplasm. Nucleus. Golgi apparatus.

Diseases

• Neoplasms
• Malignant Neoplasms
• Cell Transformation, Neoplastic
• Leukemia
• Lymphoma
• Retinoblastoma
• Myeloproliferative Disease
• Growth Retardation
• Spinal Muscular Atrophy
• Atrophy
• Janiceps
• Hyperplasia
• Lung Neoplasms

• Muscular Atrophy
• Seminoma
• Adenocarcinoma
• Fibrolamellar Carcinoma
• Malignant Neoplasm Of Lung
• Malignant Neoplasm Of Prostate
• Tissue Adhesions

Interacting Proteins

• Ajuba
• CDYL2
• CLNS1A
• COPRS
• DNMT3A

• E2F1
• GRHL3
• GTPBP2
• HIST1H4A
• HOXA9

• NUDCD2
• POLR2A
• RBM23
• RIOK1
• SRGAP2

• TRIB3
• WDR77
• YWHAZ

Pathways

• Methylation
• Localization
• Cell Proliferation
• Cell Cycle
• Cell Growth
• Rna Processing
• Histone Arginine Methylation
• Dna Methylation
• Protein Methylation
• Histone Methylation
• Chromatin Remodeling
• Dna Repair
• Translation

• Gene Silencing
• Cell Development
• Rna Interference
• Germ Cell Development
• Histone Modification
• Oogenesis
• Pathogenesis

PTMs

• Methylation
• Phosphorylation
• Acetylation
• Reduction

• Deacetylation
• Cleavage
• Demethylation
• Hydroxylation

• Glycosylation

Research Areas

• Cell Cycle and Replication
• Chromatin Research
• Circadian Rhythm

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/PRMT5

Best Uses Of The PRMT5 Marker

PRMT5 is a marker which promotes lymphatic metastasis. PRMT5 is overexpressed in cancer cells, which led to an rise in metastasis-related indicators like N-cadherin and E. This is because PRMT5 increases lymph-node invasion and metastasis. Boster Bio: PRMT5 marker - Best Uses & Applications - More Information

PICOKINE(tm)

PRMT5 is found in many biological systems when you study it. It is a protein that is expressed by brain cells as well as other areas. Researchers use this marker to determine the expression of specific proteins in cancer cells. Boster Bio offers ELISA kits as well as research antibodies to detect PRMT5 as well as other biomarkers used in the fields of neuroscience, cancer, inflammation, and development biology. These kits are very sensitive, and the sensitivity is at the picogram level. These products can be purchased from Boster Bio as well as tebubio.

PRMT5 plays a role in laryngeal cancer progression. It also influences the expression of b-catenin. In addition to affecting laryngeal cancer progression PRMT5 can also facilitate lymph-node metastasis. It also inhibits the growth and spread of lung cancer cells. To fully understand the role of PRMT5 in cancer, read on to discover more about its clinical potential.

ELISA Kit

Boster Bio PRMT5 ELISA Kit uses antibodies for detection of Band 4.1-like proteins 3. These antibodies are monoclonal, polyclonal and highly specific for this protein. The Boster kit can detect Band 4.1-like protein 3, which is found in many animals. Boster Bio developed this PRMT5 ELISA kit by using mouse and rabbit antibodies.

This ELISA kit is able to detect human, mouse, and rat PRMT5 proteins. The Boster PRMT5 ELISA kit contains the reagents and antibodies that are required for the test. In order for the ELISA to work correctly, the Boster Bio PRMT5 ELISA kit should be used in combination with the human alpha-1-antitrypsin ELISA kit.

Human chondrocytes were grown in DMEM/F-12 medium with no bovine fetus and transduced with the PRMT5 cDNA. Cell lysates were centrifuged at 10,000g for 20 minutes. Twenty micrograms of total cellular protein were loaded onto SDS-polyacrylamide gels of 10. Once transduced human chondrocytes, they were harvested 72 hours after infection with the virus vector.

Boster Bio PRMT5 ELISA Kit can be used in conjunction with other assays which measure this enzyme. This ELISA kit utilizes antibodies that have been tested against known positive and negative samples. It can provide precise results with a shorter time. When compared to other PRMT5 ELISA kits and other kits, the Boster PRMT5 ELISA Kit offers the most precise results. The results of this test are accessible to researchers from all over the world.

Boster Bio PRMT5 ELISA Kit results show that PRMT5 regulates NF-kB. It regulates osteoclast differentiation through TRAIL. It also plays a role in the dimethylation R30 of the p65 subunit. These results indicate that PRMT5 plays a significant component of the NF-kB pathway.

Proliferation of cells

The PRMT5 gene is a methyltransferase of type II that symmetrically di- or mono-methylates substrates. Conserved residues in the Rossman fold and b-barreldomain of PRMT5 aid in the methyltransferase function. The H4 molecule binds the tunnel-like region of tryptophane, phenylalanine , and leucine.

It was previously reported that the PRMT5 gene is able to incite cell proliferation in cancer cells. In this study, knockdown of PRMT5 inhibited the proliferation of HuH-7 cells under conditions of high glucose while overexpression of PRMT5 encouraged cell proliferation in HCC cells under glucose induction. It is a possibility for further research into cancer but its potential applications are limited. It is important to be cautious when manipulating the cell cycle by using PRMT5 gene-targetingRNA (shRNA).

In a recent study researchers from the University of Texas Medical Center, Dallas, Texas, and Columbia University in New York City found a link between high levels of PRMT5 as well as a poor prognosis in lung cancer. It also has a connection to neurodegenerative diseases , such as cancer and neurodegenerative disorders. Research into the function of the gene in the process of tumorigenesis and growth has led to a number of promising therapeutic targets.

PRMT5 plays a crucial role in cell proliferation and differentiation . It is also a key regulator of cell cycle that helps in the process of oncogenesis. In addition, it hinders the recruitment of T-cells. Inhibiting the expression of PRMT5 may increase the response of tumors to ICT. Genetic inhibition of PRMT5 may enhance the ICT-insensitive cold melanoma response to anti-PD1 therapy.

Cell survival

Cell survival using the PRMT5 marker is vital for EBV infection. The virus targets genes that have properties that suppress tumors. the ability to sustain PRMT5 activity is crucial for the development of a malignant character. It has been proven that the PRMT5 gene could play a role in the pathogenesis of EBV-driven B-cell transformation. To determine if this gene is necessary in the survival of B cells, researchers conducted a genome-wide mapping of chromatin from DLBCL cells. They identified multiple tumor suppressor genes implicated in EBV-driven B cell transformation with an antibody specific for this purpose. They also discovered that PRMT5 expression was associated with dephosphorylation kinases that regulate B cell receptor signaling.

Researchers conducted an investigation of pancreatic cancer cells to determine if PRMT5 regulates the activity of Myc. PRMT5 expression was linked to increased glucose uptake and lactate secretion. The effects of PRMT5 expression and FBW7 mutations on glucose uptake and lactate secretion were reduced through co-transfection. The results were validated by ECAR measurement.

PRMT5 expression was observed to predict disease progression and a poor prognosis for pancreatic cancer patients. The higher expression of PRMT5 was associated with lower survival rates for patients who are not diagnosed with cancer and shorter overall survival rates than lower levels of the protein. These results are in line with previous studies and could prove beneficial in the development of new therapies for patients with pancreatic cancer. Further research is required to identify the role of PRMT5 in the FBW7-related process.

Protein arginine and methyltransferases (PRMTs) are essential in the process of oncogenesis and cancer progression. However, the physiological role of PRMTs has been rarely investigated, but it has been proven to predict overall survival in pancreatic cancer. Additionally, PRMT5 blocks the expression of tumor suppressor gene FBW7 by stabilizing the protein cMyc. This contributes to the growth and proliferation of pancreatic cancer cell lines.