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AB151321

Anti-PRMT5 antibody

5

(1 Review)

|

(1 Publication)

Rabbit Polyclonal PRMT5 antibody. Suitable for WB, ICC/IF, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human PRMT5 aa 250-550.

View Alternative Names

HRMT1L5, IBP72, JBP1, SKB1, PRMT5, Protein arginine N-methyltransferase 5, 72 kDa ICln-binding protein, Histone-arginine N-methyltransferase PRMT5, Jak-binding protein 1, Shk1 kinase-binding protein 1 homolog, SKB1 homolog, SKB1Hs

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PRMT5 antibody (AB151321)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PRMT5 antibody (AB151321)

Immunohistochemical analysis of paraffin-embedded Human Mahlavu xenograft labeling PRMT5 with ab151321 at 1/100 dilution.

Immunocytochemistry/ Immunofluorescence - Anti-PRMT5 antibody (AB151321)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-PRMT5 antibody (AB151321)

Immunofluorescent analysis of paraformaldehyde-fixed A431 cells labeling PRMT5 with ab151321 at 1/200 dilution. Lower image co-stained with Hoechst 33342.

Western blot - Anti-PRMT5 antibody (AB151321)
  • WB

Unknown

Western blot - Anti-PRMT5 antibody (AB151321)

7.5% SDS PAGE

All lanes:

Western blot - Anti-PRMT5 antibody (ab151321) at 1/1000 dilution

All lanes:

Raji whole cell lysate at 30 µg

Predicted band size: 73 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, ICC/IF, IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human PRMT5 aa 250-550. The exact immunogen used to generate this antibody is proprietary information.

O14744

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: 20% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PRMT5 also known as Protein Arginine Methyltransferase 5 is an enzyme with molecular weight approximately 72 kDa. This protein catalyzes symmetric dimethylation of arginine residues on target proteins affecting gene expression and signal transduction. PRMT5 is expressed in various tissues with significant presence in the brain pancreas and lung. It enhances methyltransferase activity by interacting with other proteins and substrates.
Biological function summary

PRMT5 influences numerous cellular processes including RNA processing signal transduction and DNA repair. It functions as part of a protein complex often involving MEP50/WDR77 which modulates its methylating activity on histones and other proteins. This interaction dictates the cellular roles that are central to maintaining normal cellular function and regulation.

Pathways

PRMT5 operates within the Wnt/β-catenin signaling and mTOR pathways among others. As it modulates the methylation of transcription factors and regulators it contributes to transcriptional repression or activation which is important for cellular proliferation and differentiation. PRMT5 interacts with proteins such as Smad7 and cyclin D1 influencing these signaling pathways.

PRMT5 shows significant associations with cancer and neurological disorders. Elevated levels of PRMT5 correlate with the progression of various cancers including lung and breast cancers making it a potential target for therapeutic intervention. Additionally PRMT5's interaction with oncogenic proteins like MYC and MDM4 highlights its role in tumorigenesis. Furthermore PRMT5 dysregulation is linked to neurodegenerative diseases impacting the protein's target specificity and exacerbating disease symptoms.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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 : 21081503, PubMed : 21258366, PubMed : 21917714, PubMed : 22269951). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles (PubMed : 11747828, PubMed : 12411503, PubMed : 17709427). Methylates SUPT5H and may regulate its transcriptional elongation properties (PubMed : 12718890). May methylate the N-terminal region of MBD2 (PubMed : 16428440). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation (PubMed : 21258366, PubMed : 21917714). Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed : 21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 (PubMed : 22269951). Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (PubMed : 20810653). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation (PubMed : 20421892). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed : 25284789). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed : 26700805). Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression (PubMed : 25092918). Symmetrically methylates NCL (PubMed : 21081503). Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity (PubMed : 19011621). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity).
See full target information PRMT5

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

The Journal of biological chemistry 293:17769-17779 PubMed30282801

2018

Sirtuin 7-mediated deacetylation of WD repeat domain 77 (WDR77) suppresses cancer cell growth by reducing WDR77/PRMT5 transmethylase complex activity.

Applications

Unspecified application

Species

Unspecified reactive species

Hao Qi,Xiaoyan Shi,Miao Yu,Boya Liu,Minghui Liu,Shi Song,Shuaiyi Chen,Junhua Zou,Wei-Guo Zhu,Jianyuan Luo
View all publications

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