RNGTT Human

RNA Guanylyltransferase And 5'-Phosphatase Human Recombinant
Cat. No.
BT1229
Source
Escherichia Coli.
Synonyms
RNA Guanylyltransferase And 5'-Phosphatase, CAP1A, RNA Guanylyltransferase And 5-Phosphatase, HCAP1, HCE1, HCE, MRNA-Capping Enzyme, HCAP 3, mRNA-capping enzyme.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 85.0% 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.
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Description

RNGTT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 620 amino acids (1-597a.a) and having a molecular mass of 70.9kDa.
RNGTT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
RNA Guanylyltransferase And 5'-Phosphatase, also known as RNGTT, is a bifunctional enzyme responsible for mRNA capping. It exhibits RNA 5'-triphosphatase activity at its N-terminal region and mRNA guanylyltransferase activity at its C-terminal region. RNGTT catalyzes the initial two steps of cap formation: removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to create a diphosphate end, and transferring the GMP moiety from GTP to the 5'-diphosphate terminus.
Description
Recombinant human RNGTT, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 620 amino acids (1-597a.a). It has a molecular weight of 70.9 kDa. This RNGTT protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The RNGTT protein solution is provided at a concentration of 0.25 mg/ml and contains 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 40% glycerol, 2mM DTT, and 0.1mM PMSF.
Stability
For short-term storage (up to 2-4 weeks), store the solution at 4°C. For extended storage, freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 85.0% by SDS-PAGE analysis.
Synonyms
RNA Guanylyltransferase And 5'-Phosphatase, CAP1A, RNA Guanylyltransferase And 5-Phosphatase, HCAP1, HCE1, HCE, MRNA-Capping Enzyme, HCAP 3, mRNA-capping enzyme.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAHNKIP PRWLNCPRRG QPVAGRFLPL KTMLGPRYDS QVAEENRFHP SMLSNYLKSL KVKMGLLVDL TNTSRFYDRN DIEKEGIKYI KLQCKGHGEC PTTENTETFI RLCERFNERN PPELIGVHCT HGFNRTGFLI CAFLVEKMDW SIEAAVATFA QARPPGIYKG DYLKELFRRY GDIEEAPPPP LLPDWCFEDD EDEDEDEDGK KESEPGSSAS FGKRRKERLK LGAIFLEGVT VKGVTQVTTQ PKLGEVQQKC HQFCGWEGSG FPGAQPVSMD KQNIKLLDLK PYKVSWKADG TRYMMLIDGT NEVFMIDRDN SVFHVSNLEF PFRKDLRMHL SNTLLDGEMI IDRVNGQAVP RYLIYDIIKF NSQPVGDCDF NVRLQCIERE IISPRHEKMK TGLIDKTQEP FSVRNKPFFD ICTSRKLLEG NFAKEVSHEM DGLIFQPTGK YKPGRCDDIL KWKPPSLNSV DFRLKITRMG GEGLLPQNVG LLYVGGYERP FAQIKVTKEL KQYDNKIIEC KFENNSWVFM RQRTDKSFPN AYNTAMAVCN SISNPVTKEM LFEFIDRCTA ASQGQKRKHH LDPDTELMPP PPPKRPRPLT.

Product Science Overview

Gene and Protein Structure

The RNGTT gene is located on chromosome 6q15 and encodes a protein of 597 amino acids . The enzyme has two distinct functional domains:

  1. N-terminal domain: Exhibits RNA 5’-triphosphatase activity, which removes the gamma-phosphate from the 5’-triphosphate end of nascent RNA.
  2. C-terminal domain: Exhibits guanylyltransferase activity, which transfers a GMP moiety from GTP to the 5’-diphosphate terminus of RNA, forming a cap structure .
Functional Significance

The capping enzyme plays a pivotal role in coupling transcription and mRNA processing. It binds selectively to the elongating form of RNA polymerase II, where the largest subunit contains a phosphorylated C-terminal domain . This interaction ensures that capping occurs co-transcriptionally, which is vital for the proper processing and function of mRNA .

Cloning and Expression

The human RNGTT gene was identified by screening a HeLa cell library using a mouse cDNA probe. The predicted human and mouse proteins share 95% identity, indicating a high degree of conservation across species . The enzyme is expressed in all human tissues tested, highlighting its fundamental role in cellular processes .

Recombinant Protein

Recombinant HCE1 protein has been shown to display both RNA 5’-triphosphatase and guanylyltransferase activities. It can form a cap structure at the 5’-triphosphate end of RNA, which is essential for mRNA stability and function . The recombinant protein has been used in various research applications to study mRNA capping and its implications in gene expression regulation .

Clinical Relevance

Mutations or dysregulation of the RNGTT gene can have significant implications for human health. For example, RNGTT is associated with diseases such as Subserous Uterine Fibroid and Machado-Joseph Disease . Understanding the function and regulation of this enzyme can provide insights into the molecular mechanisms underlying these conditions and potentially lead to therapeutic interventions .

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