Analytical Data
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Gene name
NARS
- Application
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Alternative Names
NARS1;NARS;NRS;Asparagine--tRNA ligase. cytoplasmic
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43776
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Expression Region
1-548aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMVLAELYVSDREGSDATGDGTKEKPFK TGLKALMTVGKEPFPTIYVDSQKENERWNVISKSQLKNIKKMWHREQMKS ESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGALEGYRGQR VKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTES SVAVYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVD VQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQ VEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSR TRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIVHEL NPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIPEAPERLM TDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSM RIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWI LNRYHIRDVCLYPRFVQRCTP
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Molecular Weight
65 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
NARS (Asparaginyl-tRNA synthetase) is an essential enzyme that plays a critical role in protein synthesis by charging transfer RNA (tRNA) with the amino acid asparagine. Understanding the structural and functional dynamics of NARS is crucial, as it contributes to the fidelity of protein translation and cellular homeostasis. Notably, the dysregulation or mutations in NARS have been implicated in various diseases, including certain types of cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. Recent advancements in recombinant protein technology have enabled researchers to produce high-quality NARS for detailed biochemical and structural analyses. By utilizing techniques such as X-ray crystallography and cryo-electron microscopy, scientists aim to elucidate the enzyme's mechanism, interactions with tRNA, and regulatory pathways. This research not only sheds light on the fundamental processes of gene expression and cellular function but also opens avenues for the development of novel drugs that can modulate NARS activity in pathological conditions. The study of NARS thus stands at the intersection of molecular biology, biochemistry, and therapeutic innovation, underscoring its significance in both basic and applied sciences.











