RNMT Human

RNA (guanine-7-) Methyltransferase Human Recombinant
Cat. No.
BT13245
Source
Escherichia Coli.
Synonyms

mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.

Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

RNMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-476 a.a.) and having a molecular mass of 57kDa.
RNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
RNMT, a member of the mRNA cap methyltransferase family, is a nuclear protein found in many cell types. It plays a crucial role in cap-dependent mRNA translation by methylating the guanosine cap of mRNA. Specifically, RNMT catalyzes the transfer of a methyl group from S-adenosylmethionine (AdoMet) to the N-7 position of the GpppN end of growing mRNA, resulting in the formation of S-adenosylhomocysteine (AdoHyc) and m7GpppN-terminated RNA.
Description
Produced in E. coli, recombinant human RNMT is a single, non-glycosylated polypeptide chain consisting of 496 amino acids (specifically, amino acids 1 to 476). It has a molecular mass of 57 kDa. The protein is fused to a 20 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
The product is a clear, sterile-filtered solution without any color.
Formulation
This solution contains 0.5mg/ml of RNMT in a buffer composed of 20mM Tris-HCl (pH 8.0), 2mM DTT, 20% glycerol, and 100mM NaCl.
Stability
While RNMT Human Recombinant remains stable for up to 1 week at 4°C, it is recommended to store it at temperatures below -18°C to ensure its long-term stability. Avoid repeated freezing and thawing of the product.
Purity
The purity of this product is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms

mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MANSAKAEEY EKMSLEQAKA SVNSETESSF NINENTTASG TGLSEKTSVC RQVDIARKRK EFEDDLVKES SSCGKDTPSK KRKLDPEIVP EEKDCGDAEG NSKKRKRETE DVPKDKSSTG DGTQNKRKIA LEDVPEKQKN LEEGHSSTVA AHYNELQEVG LEKRSQSRIF YLRNFNNWMK SVLIGEFLEK VRQKKKRDIT VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSVKQCQQRY EDMKNRRDSE YIFSAEFITA DSSKELLIDK FRDPQMCFDI CSCQFVCHYS FESYEQADMM LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD YPLFGCKYDF NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE EKIKNNENKM LLKRMQALEP YPANESSKLV SEKVDDYEHA AKYMKNSQVR LPLGTLSKSE WEATSIYLVF AFEKQQ.

Product Science Overview

Structure and Function

RNMT is a protein encoded by the RNMT gene in humans. The enzyme consists of 476 amino acids and has a molecular weight of approximately 55 kDa . The catalytic domain of RNMT lies between residues 121–476, and this domain is conserved in sequence, structure, and function across various eukaryotic species . The N-terminal domain (1–120 amino acids) is not required for catalytic activity but plays a regulatory role by facilitating the recruitment of RNMT to RNA polymerase II transcription initiation sites .

Mechanism of Action

The capping process of mRNA involves three sequential enzymatic activities: triphosphatase, guanylyltransferase, and methyltransferase . RNMT catalyzes the final step of this process, where it transfers a methyl group from S-adenosyl methionine (AdoMet) to the N7 position of the guanine nucleotide, forming the mature cap structure, 7-methylguanosine (m7GpppN) . This cap structure is critical for the recognition of mRNA by the cap-binding complex and eukaryotic initiation factor 4F, which are involved in splicing, export, and translation initiation .

Biological Significance

The 5’ cap structure of mRNA is essential for several cellular processes:

  • Protection from Degradation: The cap structure protects mRNA from degradation by exonucleases during transcription .
  • Translation Efficiency: The cap enhances the efficiency of translation by facilitating the binding of ribosomes to the mRNA .
  • Splicing and Export: The cap structure is involved in the splicing of pre-mRNA and the export of mature mRNA from the nucleus to the cytoplasm .
Clinical and Therapeutic Implications

RNMT has been implicated in the proliferation of cancer cells and is considered a potential target for the development of anticancer therapeutics . Additionally, coronaviruses mimic the capping process of mRNA to evade the human immune system, making RNMT a target for the development of antiviral therapeutics . The enzyme’s role in mRNA stability and translation makes it a critical factor in cellular growth and proliferation.

Research and Development

Recent studies have focused on the kinetic characterization of human RNMT and the development of assays for high-throughput screening of potential inhibitors . These efforts aim to discover chemical probes and inhibitors that can be used to further investigate the roles of RNMT in cancer and viral infections .

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