WARS Human

Tryptophanyl-tRNA Synthetase Human Recombinant
Cat. No.
BT28112
Source
Escherichia Coli.
Synonyms

GAMMA-2, IFI53, IFP53, WRS, WARS, TrpRS, hWRS, EC=6.1.1.2, Tryptophanyl-tRNA synthetase, INF-induced protein 53, Tryptophan--tRNA ligase, GAMMA-2.

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.
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Description

WARS Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 491 amino acids (1-471 a.a.) and having a molecular mass of 55.3 kDa. The WARS is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Tryptophanyl-tRNA synthetase (WARS) is an enzyme that plays a crucial role in protein synthesis. It belongs to the class I tRNA synthetase family. There are two types of tryptophanyl tRNA synthetase: a cytoplasmic form (WARS) and a mitochondrial form (WARS2). WARS catalyzes the attachment of the amino acid tryptophan to its corresponding tRNA molecule, tRNA(trp). This process, known as aminoacylation, is essential for the translation of genetic information from mRNA to protein. WARS is induced by interferon (INF) and has been implicated in various cellular processes, including angiogenesis, cytoskeletal reorganization, and shear stress-responsive gene expression. It exerts these effects by regulating the activity of signaling pathways involving ERK, Akt, and eNOS.
Description
Recombinant Human WARS, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 491 amino acids, with amino acids 1-471 representing the WARS sequence. The protein has a molecular mass of 55.3 kDa. For purification and detection purposes, a 20 amino acid His-Tag is fused to the N-terminus of WARS. The protein is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The solution contains 1mg of WARS per ml. It is buffered with 20mM Tris-HCl at pH 8 and also contains 1mM DTT, 0.1M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution can be stored at 4°C. For long-term storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein like HSA or BSA to a final concentration of 0.1% is advisable for long-term storage. To maintain the protein's integrity, avoid repeated freezing and thawing cycles.
Purity
The purity of WARS is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms

GAMMA-2, IFI53, IFP53, WRS, WARS, TrpRS, hWRS, EC=6.1.1.2, Tryptophanyl-tRNA synthetase, INF-induced protein 53, Tryptophan--tRNA ligase, GAMMA-2.

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY KAAAGEDYKA DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY DKLIVRFGSS KIDKELINRI ERATGQRPHH FLRRGIFFSH RDMNQVLDAY ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT KWLQDVFNVP LVIQMTDDEK YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY MGMSSGFYKN VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM SASDPNSSIF LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF MYLTFFLEDD DKLEQIRKDY TSGAMLTGEL KKALIEVLQP LIAEHQARRK EVTDEIVKEF MTPRKLSFDF Q.

Product Science Overview

Introduction

Tryptophanyl-tRNA synthetase (TrpRS) is an essential enzyme involved in the translation process of protein synthesis. It catalyzes the ligation of the amino acid tryptophan to its corresponding tRNA (tRNA^Trp), a crucial step in the translation of genetic information from mRNA to proteins .

Structure and Function

TrpRS belongs to the family of aminoacyl-tRNA synthetases (ARSs), which are responsible for the accurate pairing of amino acids with their respective tRNAs. This enzyme ensures that tryptophan is correctly incorporated into the growing polypeptide chain during protein synthesis. The reaction involves the formation of tryptophanyl-AMP from tryptophan and ATP, followed by the transfer of tryptophan to tRNA^Trp .

Physiological Roles

Beyond its canonical role in protein synthesis, TrpRS has been implicated in various physiological and pathological processes. It has been shown to play roles in immune response, angiogenesis, and apoptosis. For instance, TrpRS expression is upregulated by interferon-gamma (IFN-γ), highlighting its involvement in immune regulation .

Clinical Significance

TrpRS has garnered attention as a potential biomarker and therapeutic target in several diseases. It has been studied as a synovial biomarker for diagnosing septic arthritis, demonstrating high specificity and sensitivity in distinguishing septic arthritis from other inflammatory conditions . Additionally, TrpRS is being explored for its potential roles in cancer, autoimmune diseases, and neurodegenerative disorders .

Recombinant TrpRS

Human recombinant TrpRS is produced through recombinant DNA technology, allowing for the large-scale production of this enzyme for research and therapeutic purposes. Recombinant TrpRS retains the functional properties of the native enzyme and is used in various biochemical and clinical studies to understand its roles and develop potential therapeutic interventions.

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