Analytical Data
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Gene name
GARS
- Application
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Alternative Names
CMT2D; CMT2-D; DSMAV; GlyRS; SMAD1; EJ; Charcot-Marie-Tooth Neuropathy 2D; Glycine tRNA Ligase; Diadenosine tetraphosphate synthetase; AP-4-A synthetase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P41250
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Expression Region
Val567~Glu735
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Molecular Weight
23kDa
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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
GARS (Glycyl-tRNA synthetase) is an essential enzyme involved in the protein synthesis machinery of cells, responsible for attaching glycine to its corresponding tRNA. The study of GARS and its recombinant forms has gained traction due to its critical role in cellular function and implications in various diseases. Mutations in the GARS gene have been associated with peripheral neuropathies such as Charcot-Marie-Tooth disease, highlighting the enzyme's significance in maintaining nervous system integrity. Furthermore, GARS exhibits non-canonical functions that extend beyond its classical role in translation, including potential involvement in stress responses and cell signaling pathways. The production of recombinant GARS proteins facilitates the investigation of these diverse functions, allowing researchers to explore structure-function relationships and the mechanistic basis of GARS-related pathologies. By utilizing techniques such as site-directed mutagenesis and structural biology methods, scientists aim to elucidate how specific mutations affect GARS activity and its interactions within the cell. Understanding the molecular underpinnings of GARS could lead to novel therapeutic strategies for related diseases and provide insights into the broader implications of aminoacyl-tRNA synthetases in cellular physiology. Overall, the study of GARS recombinant proteins is pivotal not only for unraveling the complexities of protein synthesis but also for addressing the clinical challenges posed by GARS-associated disorders.
