YARS Human

Tyrosyl-tRNA Synthetase Human Recombinant
Cat. No.
BT28192
Source
Escherichia Coli.
Synonyms
Tyrosyl-tRNA synthetase cytoplasmic, Tyrosyl--tRNA ligase, TyrRS, YARS, YRS, YTS, CMTDIC.
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. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

YARS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 548 amino acids (1-528 a.a.) and having a molecular mass of 61.3kDa.
YARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Tyrosyl-tRNA synthetase (YARS) is an essential enzyme within the class I tRNA synthetase family. Its primary role is to catalyze the attachment of tryptophan to tRNATrp, a crucial step in the cell's protein synthesis process. The expression of YARS is significantly increased in human cells when IFN-gamma is introduced.
Description
Produced in E. coli, YARS is a single, non-glycosylated polypeptide chain composed of 548 amino acids (specifically, amino acids 1 to 528). It possesses a molecular mass of 61.3kDa. For purification, a 20 amino acid His-tag is fused to the N-terminus of YARS, and proprietary chromatographic techniques are employed.
Physical Appearance
A clear, colorless solution that has been sterilized through filtration.
Formulation
The YARS protein solution is provided at a concentration of 1mg/ml and contains the following components: 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, and 0.1M NaCl.
Stability
For short-term storage (2-4 weeks), keep the solution refrigerated at 4°C. For extended storage, freeze the solution at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Avoid repeated freezing and thawing.
Purity
SDS-PAGE analysis indicates a purity greater than 90.0%.
Synonyms
Tyrosyl-tRNA synthetase cytoplasmic, Tyrosyl--tRNA ligase, TyrRS, YARS, YRS, YTS, CMTDIC.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKIYW GTATTGKPHV AYFVPMSKIA DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVSYYENV IKAMLESIGV PLEKLKFIKG TDYQLSKEYT LDVYRLSSVV TQHDSKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD AQFGGIDQRK IFTFAEKYLP ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED VKKKLKKAFC EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT AYVDLEKDFA AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPM AKGPAKNSEP EEVIPSRLDI RVGKIITVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV VVLCNLKPQK MRGVESQGML LCASIEGINR QVEPLDPPAG SAPGEHVFVK GYEKGQPDEE LKPKKKVFEK LQADFKISEE CIAQWKQTNF MTKLGSISCK SLKGGNIS.

Product Science Overview

Background of Tyrosyl-tRNA Synthetase (Human Recombinant)

Introduction

Tyrosyl-tRNA synthetase (TyrRS) is an essential enzyme involved in the translation process of protein synthesis. It catalyzes the attachment of the amino acid tyrosine to its corresponding tRNA molecule, forming tyrosyl-tRNA. This process is crucial for the accurate translation of the genetic code into functional proteins. Human recombinant tyrosyl-tRNA synthetase (rhTyrRS) is a form of this enzyme that has been engineered for research and therapeutic purposes.

Structure and Function

Human TyrRS is composed of three domains:

  1. Amino-terminal Rossmann fold domain: Responsible for the formation of the activated EzTyr-AMP intermediate and is conserved among bacteria, archaea, and eukaryotes.
  2. tRNA anticodon recognition domain: This domain is not conserved between bacteria and eukaryotes.
  3. Carboxyl-terminal domain: Unique to human TyrRS, this domain shares significant sequence homology with other proteins such as the putative human cytokine endothelial monocyte-activating protein II .

Biological Significance

TyrRS plays a critical role in protein synthesis by ensuring the correct amino acid is incorporated into the growing polypeptide chain. Beyond its canonical role in translation, TyrRS has been implicated in various cellular processes, including cell signaling and immune responses. For instance, proteolytic removal of the C-domain from TyrRS activates its cytokine function .

Recombinant Human TyrRS

Recombinant human TyrRS (rhTyrRS) is produced using genetic engineering techniques. The gene encoding human TyrRS is cloned into an expression vector, which is then introduced into a host organism such as Escherichia coli. The host organism expresses the TyrRS protein, which is subsequently purified for research or therapeutic use .

Applications and Research

rhTyrRS has been utilized in various research studies to understand its role in disease and potential therapeutic applications. For example, autoantibodies against TyrRS have been associated with anti-synthetase syndrome, a condition characterized by myositis, arthritis, and interstitial lung disease . Additionally, rhTyrRS has been explored as a potential target for developing new antimicrobial agents, particularly against drug-resistant strains of Mycobacterium tuberculosis .

Conclusion

Tyrosyl-tRNA synthetase is a vital enzyme with significant roles in protein synthesis and cellular signaling. The recombinant form of this enzyme, rhTyrRS, has opened new avenues for research and therapeutic applications, highlighting its importance in both basic and applied sciences.

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