AsnRS

Asparagine tRNA Synthetase Brugia Malayi Recombinant
Cat. No.
BT25645
Source
Escherichia Coli.
Synonyms
Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% 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

AsnRS Brugia Malayi Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 568 amino acids (including a 6xHis Tag at N-terminus) and having a molecular mass of 64.5kDa.
The AsnRS is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Asparaginyl-tRNA synthetase (AsnRS) belongs to the ligase family of enzymes and plays a crucial role in protein synthesis. Specifically, it catalyzes the attachment of the amino acid asparagine to its cognate transfer RNA (tRNAAsn). This enzymatic reaction involves the substrates ATP, L-asparagine, and tRNA(Asn), resulting in the formation of AMP, diphosphate, and L-asparaginyl-tRNA(Asn).
Description
Recombinant AsnRS from Brugia Malayi, expressed in E.Coli, is a monomeric polypeptide chain with a molecular weight of 64.5kDa. It comprises 568 amino acids, including an N-terminal 6xHis Tag for purification purposes. The AsnRS protein has undergone purification using proprietary chromatographic techniques and lacks glycosylation.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The AsnRS protein is supplied as a 0.2µm filtered solution in a buffer consisting of 20mM HEPES (pH 7.4), 100mM NaCl, 5mM MgCl2, 5mM β-Mercaptoethanol, and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), maintain the AsnRS solution at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein such as HSA or BSA (0.1%) is advisable. Repeated freezing and thawing of the AsnRS solution should be avoided.
Purity
The purity of the AsnRS protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTVYICPETG DDGNDGSELK PLRTLYQAMI ITKSSKGDFL IRTKKDGKQV WEAASKTALK KSWKRYEQEM LKNEKVAAKM LEKDATEVGV KAALEEAKKV QIELDTSLSY ITGVKIRDLV KHRNERVCIK GWIHRMRRQG KSLMFFILRD GTGFLQVLLM DKLCQTYDAL TVNTECTVEI YGAIKEVPEG KEAPNGHELI ADFWKIIGNA PSGGIDNVLN EEASVDKMLD NRHLVIRGEN AAALLRLRAA ATRAMREHFY NAGYVEVAPP TLVQTQVEGG STLFNLDYFG EQSFLTQSSQ LYLETCIPTL GDVFLHCSVL QGGKISHSST LAEYAHVEAE CPFITLDDLM EKIEELVCDT VDRLLADEEA KKLLEHINPK FQPPERPFLR MEYKDAIKWL QEHNVENEFG NTFTYGEDIA EAAERFMTDT INKPILLNRF PSEIKAFYMQ RDAKDNTLTE SVDLLMPGVG EIVGGSMRIW KFDELSKAFK NVEIDPKPYY WYLDQRLYGT CPHGGYGLGL ERFICWLTNT NHIRDVCLYP RFVGRCVP.

Product Science Overview

Introduction

Asparagine tRNA synthetase (AsnRS) is an enzyme that plays a crucial role in protein synthesis by attaching the amino acid asparagine to its corresponding tRNA molecule. This process, known as aminoacylation, is essential for the accurate translation of genetic information into proteins. The recombinant form of AsnRS from Brugia malayi, a parasitic nematode, has garnered significant interest due to its unique properties and potential applications in biomedical research.

Brugia malayi and Lymphatic Filariasis

Brugia malayi is one of the causative agents of lymphatic filariasis, a debilitating disease that affects millions of people worldwide. This parasitic infection leads to severe swelling and disfigurement, commonly known as elephantiasis. Understanding the molecular biology of Brugia malayi is crucial for developing effective treatments and interventions for this disease.

Structure and Function of AsnRS

The AsnRS enzyme from Brugia malayi is a single, non-glycosylated polypeptide chain consisting of 568 amino acids, including a 6xHis tag at the N-terminus, and has a molecular mass of approximately 64.5 kDa . This enzyme is responsible for catalyzing the attachment of asparagine to its corresponding tRNA, a critical step in protein synthesis.

Recombinant AsnRS Production

Recombinant AsnRS from Brugia malayi is typically produced in Escherichia coli (E. coli) using advanced chromatographic techniques to ensure high purity and activity . The recombinant form allows researchers to study the enzyme in detail and explore its potential applications in various fields, including drug development and immunology.

Biological Significance

Research has shown that Brugia malayi AsnRS acts as a physiocrine, binding specifically to interleukin-8 (IL-8) chemokine receptors on endothelial cells . This interaction stimulates endothelial cell proliferation, vasodilation, and angiogenesis, which are processes involved in the pathology of lymphatic filariasis . The enzyme’s ability to mimic the effects of vascular endothelial growth factor (VEGF) highlights its potential as a target for therapeutic intervention .

Potential Applications

The unique properties of Brugia malayi AsnRS make it a valuable tool for biomedical research. By studying this enzyme, scientists can gain insights into the molecular mechanisms underlying lymphatic filariasis and develop new strategies for treatment. Additionally, the enzyme’s role in endothelial cell function suggests potential applications in vascular biology and regenerative medicine.

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