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PRMT5/MEP50 Complex Human Recombinant

Original price was: $2,395.00.Current price is: $1,195.00.

Catalog Number: B2016867 (20 µg)
PRMT5/MEP50 Complex Human Recombinant is a high quality protein complex composed of protein arginine methyltransferase 5 (PRMT5) and its cofactor MEP50. PRMT5 is an enzyme that catalyzes the methylation of arginine residues on target proteins, while MEP50 is a regulatory subunit that enhances the catalytic activity of PRMT5. This complex plays a role in various cellular processes, including gene expression regulation, RNA processing, and cell signaling. The human recombinant PRMT5/MEP50 complex is a purified form of this protein complex that is produced using recombinant DNA technology for research purposes. This product has been used as a molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

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Product Description

PRMT5/MEP50 Complex Human Recombinant
Catalog number: B2016867
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 20 µg
Molecular Weight or Concentration: 73 (PRMT5) and 37.5 (MEP50) kDa
Supplied as: Solution
Applications: a molecular tool for various biochemical applications
Storage: -80°C
Keywords: Histone-arginine N-methyltransferase PRMT5, IBP72, Jak-binding Protein 1, JBP1, Protein-arginine N-methyltransferase 5, Shk1 Kinase-binding protein 1 Homolog, SKB1 Homolog, 72 kDa ICIn-binding Protein
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: Eddershaw AR, Stubbs CJ, Edwardes LV, Underwood E, Hamm GR, Davey PRJ, Clarkson PN, Syson K. Characterization of the Kinetic Mechanism of Human Protein Arginine Methyltransferase 5 Biochemistry. 2020 Dec 22;59(50):4775-4786.
2: Antonysamy S. The Structure and Function of the PRMT5:MEP50 Complex Subcell Biochem. 2017;83:185-194.
3: Stopa N, Krebs JE, Shechter D. The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond Cell Mol Life Sci. 2015 Jun;72(11):2041-59.
4: Timm DE, Bowman V, Madsen R, Rauch C. Cryo-electron microscopy structure of a human PRMT5:MEP50 complex PLoS One. 2018 Mar 8;13(3):e0193205.
5: Antonysamy S, Bonday Z, Campbell RM, Doyle B, Druzina Z, Gheyi T, Han B, Jungheim LN, Qian Y, Rauch C, Russell M, Sauder JM, Wasserman SR, Weichert K, Willard FS, Zhang A, Emtage S. Crystal structure of the human PRMT5:MEP50 complex Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17960-5.
6: Krzyzanowski A, Gasper R, Adihou H, Hart P’, Waldmann H. Biochemical Investigation of the Interaction of pICln, RioK1 and COPR5 with the PRMT5-MEP50 Complex Chembiochem. 2021 Jun 2;22(11):1908-1914.
7: Saha K, Fisher ML, Adhikary G, Grun D, Eckert RL. Sulforaphane suppresses PRMT5/MEP50 function in epidermal squamous cell carcinoma leading to reduced tumor formation Carcinogenesis. 2017 Aug 1;38(8):827-836.
8: Ho MC, Wilczek C, Bonanno JB, Xing L, Seznec J, Matsui T, Carter LG, Onikubo T, Kumar PR, Chan MK, Brenowitz M, Cheng RH, Reimer U, Almo SC, Shechter D. Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity PLoS One. 2013;8(2):e57008.
9: Yang XC, Desotell A, Lin MH, Paige AS, Malinowska A, Sun Y, Aik WS, Dadlez M, Tong L, Dominski Z. In vitro methylation of the U7 snRNP subunits Lsm11 and SmE by the PRMT5/MEP50/pICln methylosome RNA. 2023 Nov;29(11):1673-1690.
10: Chen H, Lorton B, Gupta V, Shechter D. A TGFβ-PRMT5-MEP50 axis regulates cancer cell invasion through histone H3 and H4 arginine methylation coupled transcriptional activation and repression Oncogene. 2017 Jan 19;36(3):373-386.

Products Related to PRMT5/MEP50 Complex Human Recombinant can be found at Proteins

Additional Information

Weight 48 oz
Dimensions 8 × 8 × 8 in

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