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AB167953

Recombinant human PRMT3 protein

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(1 Publication)

Recombinant human PRMT3 protein is a Human Full Length protein, in the 1 to 531 aa range, expressed in Baculovirus infected Sf9 cells, with >90%, suitable for SDS-PAGE, WB, FuncS.

View Alternative Names

HRMT1L3, PRMT3, Protein arginine N-methyltransferase 3, Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3

2 Images
Functional Studies - Recombinant human PRMT3 protein (AB167953)
  • FuncS

Unknown

Functional Studies - Recombinant human PRMT3 protein (AB167953)

The specific activity of ab167953 was determined to be 12 nmol/min/mg as per activity assay protocol.

SDS-PAGE - Recombinant human PRMT3 protein (AB167953)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PRMT3 protein (AB167953)

SDS-PAGE analysis of ab167953.

Key facts

Purity

>90% Densitometry

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

WB, FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

The specific activity of ab167953 was determined to be 12 nmol/min/mg as per activity assay protocol.

Accession

O60678

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.004% EDTA, 0.002% PMSF

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIKHIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKSKKDPRSLTVTLTLNNSTQTYGLQ","proteinLength":"Full Length","predictedMolecularWeight":"97 kDa","actualMolecularWeight":null,"aminoAcidEnd":531,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Baculovirus infected Sf9 cells","accessionNumber":"O60678","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

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

Protein arginine methyltransferase 3 (PRMT3) plays an important role in the methylation of arginine residues on various substrates which influences protein-protein interactions signal transduction and gene expression. Also known as HRMT1L3 PRMT3 has an approximate molecular weight of 59 kDa. Researchers find this enzyme mainly in the cytoplasm although it can also localize in the nucleus. Expression of PRMT3 happens across multiple tissues with notable presence in the liver and lungs.
Biological function summary

PRMT3 methylates ribosomal protein S2 an activity that suggests its participation in ribosome assembly and nucleolar functions. It forms a complex with ribosomal proteins and several metabolic enzymes which highlight its involvement in protein synthesis and cellular metabolic regulation. The activity of PRMT3 regulates the biogenesis of ribosomes which are central to protein production in cells.

Pathways

PRMT3 influences various cellular processes like the ribosome biogenesis and the mTOR signaling pathway. Its interaction with the ribosome synthesis pathway aids in the maturation and assembly of ribosomal subunits. In the mTOR pathway PRMT3 relates to S6 kinase and eukaryotic initiation factors affecting cell growth and metabolism through the regulation of protein synthesis.

PRMT3 may influence the development of metabolic syndromes and certain cancers. Studies suggest a potential link between PRMT3 dysregulation and the onset of insulin resistance making it significant in the context of type 2 diabetes. Additionally abnormal PRMT3 expression connects with progression of malignancies potentially through interacting with oncogenic proteins and altering signaling pathways that regulate cell cycle and apoptosis.
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Specifications

Form

Liquid

Additional notes

Affinity purified.

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General info

Function

Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (Probable). May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity (PubMed : 33495566).

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.

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Product protocols

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Target data

Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (Probable). May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity (PubMed : 33495566).
See full target information PRMT3
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Publications (1)

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

Cancers 11: PubMed30577570

2018

Protein Arginine Methyltransferase 3 Enhances Chemoresistance in Pancreatic Cancer by Methylating hnRNPA1 to Increase ABCG2 Expression.

Applications

Unspecified application

Species

Unspecified reactive species

Ming-Chuan Hsu,Mei-Ren Pan,Pei-Yi Chu,Ya-Li Tsai,Chia-Hua Tsai,Yan-Shen Shan,Li-Tzong Chen,Wen-Chun Hung
View all publications
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