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AB202188

Recombinant Human TGT protein

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Recombinant Human TGT protein is a Human Full Length protein, in the 1 to 403 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

TGT, TGUT, QTRT1, Queuine tRNA-ribosyltransferase catalytic subunit 1, Guanine insertion enzyme, tRNA-guanine transglycosylase

1 Images
SDS-PAGE - Recombinant Human TGT protein (AB202188)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human TGT protein (AB202188)

15% SDS-PAGE analysis of ab202188 (3 μg).

Key facts

Purity

>80% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

Q9BXR0

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 69% PBS, 30% Glycerol (glycerin, glycerine), 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

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

Product details

This product was previously labelled as QTRT1

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSEFMAGAATQASLESAPRIMRLVAECSRSRARAGELWLPHGTVATPVFMPVGTQATMKGITTEQLDALGCRICLGNTYHLGLRPGPELIQKANGLHGFMNWPHNLLTDSGGFQMVSLVSLSEVTEEGVRFRSPYDGNETLLSPEKSVQIQNALGSDIIMQLDDVVSSTVTGPRVEEAMYRSIRWLDRCIAAHQRPDKQNLFAIIQGGLDADLRATCLEEMTKRDVPGFAIGGLSGGESKSQFWRMVALSTSRLPKDKPRYLMGVGYATDLVVCVALGCDMFDCVFPTRTARFGSALVPTGNLQLRKKVFEKDFGPIDPECTCPTCQKHSRAFLHALLHSDNTAALHHLTVHNIAYQLQLMSAVRTSIVEKRFPDFVRDFMGAMYGDPTLCPTWATDALASVGITLG","proteinLength":"Full Length","predictedMolecularWeight":"46.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":403,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9BXR0","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

The TGT protein also known as tRNA-guanine transglycosylase functions mechanically by modifying transfer RNA (tRNA) molecules through the exchange of guanine at specific tRNA positions with preQ1 precursors. This enzymatic activity is essential in tRNA maturation. The enzyme has a molecular mass of about 43 kDa. TGT is expressed mainly in the cytoplasm of eukaryotic cells and shows a high level of conservation across different species.
Biological function summary

The TGT catalyzed guanine exchange on tRNA enhances the correct folding of tRNA and supports the accuracy of protein translation. The protein is a part of an RNA-modifying enzyme family and does not typically form complexes but acts independently on its tRNA substrates. Its activity ensures proper tRNA structure influencing protein synthesis efficiency and overall cellular protein homeostasis.

Pathways

TGT plays an important role in the tRNA modification pathway which is important for post-transcriptional RNA processing. It connects with pathways involved in protein synthesis and RNA stability. TGT's function is integrally linked with enzymes like tRNA synthetases which are responsible for charging tRNAs with their corresponding amino acids establishing a pivotal link in the genetic code translation process.

Alterations in TGT function or expression impact specific disorders such as mitochondrial myopathy which results from defects in tRNA modification leading to flawed mitochondrial protein synthesis. TGT also has connections to cancer biology where aberrant tRNA modifications by TGT might influence tumoral cell growth and response to stress. In these contexts the interactions between TGT and other proteins involved in RNA metabolism such as Dicer point to a broader influence on cellular regulatory mechanisms linked to disease states.

Specifications

Form

Liquid

Additional notes

ab202188 was purified using conventional chromatography techniques.

General info

Function

Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed : 11255023, PubMed : 20354154, PubMed : 34009357, PubMed : 34241577). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product (By similarity). Modification of cytoplasmic tRNAs with queuosine controls the elongation speed of cognate codons, thereby ensuring the correct folding of nascent proteins to maintain proteome integrity (PubMed : 30093495).

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Subcellular localisation

Mitochondrion outer membrane

Product protocols

Target data

Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed : 11255023, PubMed : 20354154, PubMed : 34009357, PubMed : 34241577). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product (By similarity). Modification of cytoplasmic tRNAs with queuosine controls the elongation speed of cognate codons, thereby ensuring the correct folding of nascent proteins to maintain proteome integrity (PubMed : 30093495).
See full target information QTRT1

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