Analytical Data
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Gene name
GARS
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简介
The GARS protein performs ATP-dependent ligation of glycine to its tRNA, creating a Gly-AMP intermediate. It also produces diadenosine tetraphosphate (Ap4A) by condensing two ATP molecules, which is important for cellular regulation. GARS may have a specific role in maintaining Ap4A homeostasis. GARS Protein, Human (sf9, His) is the recombinant human-derived GARS protein, expressed by Sf9 insect cells , with N-His labeled tag.
- Application
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Alternative Names
Glycine--tRNA ligase; GlyRS; GARS1; GARS
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Species
Human
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Source
Baculovirus
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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
P41250-1
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Expression Region
M1-E739
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Protein Length
Full Length of Isoform-1
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Molecular Weight
85.5 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
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.
