Analytical Data
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Gene name
HARS
- Application
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Alternative Names
HARS1;HARS;HRS;Histidine--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
P12081
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Expression Region
1-509aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMAERAALEELVKLQGERVRGLKQQKAS AELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKGTRDYSPRQMAVREKVF DVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSL RYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFD IAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVS DSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGV SLVEQLLQDPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARG LDYYTGVIYEAVLLQTPAQAGEEPLGVGSVAAGGRYDGLVGMFDPKGRKV PCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKL VSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIK LRSVTSREEVDVRREDLVEEIKRRTGQPLCIC
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Molecular Weight
60 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
Related Products
Protein Description
HARS, or Histidyl-tRNA synthetase, is an essential enzyme that plays a critical role in protein synthesis by catalyzing the attachment of histidine to its corresponding tRNA. Its significance in cellular functions is underscored by its involvement in various physiological and pathological processes. Research into HARS has garnered attention due to its implications in various diseases, including neurodegenerative disorders and cancers, where its expression levels and functional integrity may be disrupted. Additionally, HARS is implicated in the regulation of aminoacyl-t RNA synthetases, and its role in the 'unfolded protein response' highlights its connection to cellular stress responses. In recent years, advances in structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, have provided deeper insights into the enzyme's structure-function relationship, contributing to our understanding of its catalytic mechanisms and interactions with other cellular components. Furthermore, HARS research has opened potential avenues for therapeutic interventions, as modulators of its activity could serve as novel strategies for treating diseases associated with its dysregulation. Overall, the study of HARS and its recombinant proteins continues to be a promising field that combines molecular biology, biochemistry, and medicine, with the potential to unlock new understanding of translational control and its impact on human health.
