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Key Documents

P0493

Sigma-Aldrich

Monoclonal Anti-PRMT5 antibody produced in mouse

~2 mg/mL, clone PRMT5-21, purified immunoglobulin, buffered aqueous solution

Sinonimo/i:

Anti-Protein-Arginine Methyl Transferase 5

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

PRMT5-21, monoclonal

Forma fisica

buffered aqueous solution

PM

antigen ~70 kDa by SDS-PAGE

Reattività contro le specie

mouse, hamster, bovine, canine, monkey, rat, human, chicken

Concentrazione

~2 mg/mL

tecniche

indirect ELISA: suitable
microarray: suitable
western blot: 2 μg/mL using whole cell extract of human melanoma cell line G361

Isotipo

IgG2a

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... PRMT5(10419)

Descrizione generale

Monoclonal Anti-PRMT5 (mouse IgG2a isotype) is derived from the PRMT5-21 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from mice immunized with GST-PRMT5 containing the C-terminal region of the human PRMT5. Protein arginine methyltransferases (PRMT) 5 belongs to the type II arginine methyltransferases. PRMT5 (also known as Skb1Hs/janus kinase-binding protein 1 (JBP1) exists as homo-oligomeric complexes, which includes a dimer and tetramer. PRMT5 is found mainly in the cytoplasm. This gene is located on human chromosome 14q11.2.

Immunogeno

GST-PRMT5 containing the C-terminal region of the human PRMT5 (amino acids 315-637).

Applicazioni

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Monoclonal Anti-PRMT5 antibody produced in mouse has been used in enzyme-linked immunosorbent assay (ELISA) and immunoblotting.

Azioni biochim/fisiol

Protein arginine methyltransferase 5 (PRMT5) participates in the symmetrical dimethylation of arginine residues. Homooligomerization of PRMT5 has an important role in its ability to methylate the myelin basic protein (MBP) protein. PRMT5 also binds the Janus kinases and are involved in an interferon-signaling pathway. It also helps to produce symmetrical ω-NG-dimethylarginine.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Raccomandato

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Descrizione
Determinazione del prezzo

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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LKB1 regulates PRMT5 activity in breast cancer
Lattouf H, et al.
International Journal of Cancer. Journal International Du Cancer, 144(3), 595-606 (2019)
Ming Liu et al.
Theranostics, 10(10), 4437-4452 (2020-04-16)
The proto-oncogene c-Myc regulates multiple biological processes mainly through selectively activating gene expression. However, the mechanisms underlying c-Myc-mediated gene repression in the context of cancer remain less clear. This study aimed to clarify the role of PRMT5 in the transcriptional
PRMT5 dimethylates R30 of the p65 subunit to activate NF-?B.
Wei H
Proceedings of the National Academy of Sciences of the USA, 110(33), 13516-13521 (2013)
Expression of protein arginine methyltransferase-5 in oral squamous cell carcinoma and its significance in epithelial-to-mesenchymal transition
Amano Y, et al.
Pathology international, 68(6), 359-366 (2018)
Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family
Rho J, et al.
The Journal of biological chemistry, 276(14), 11393-11401 (2001)

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