Analytical Data
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Gene name
GLYATL1
- Application
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Alternative Names
Acyltransferase which transfers an acyl group to the N-terminus of glutamine. Can use phenylacetyl-CoA as an acyl donor.
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q969I3
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Expression Region
1-302aa
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Molecular Weight
62.1 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
GLYATL1 (glycine N-acyltransferase 1) is an enzyme that plays a critical role in the metabolism of glycine, a non-essential amino acid involved in several physiological processes, including neurotransmission and the synthesis of crucial biomolecules. Abnormalities in glycine metabolism have been associated with various neurodevelopmental and metabolic disorders, highlighting the importance of understanding GLYATL1 function. Recent studies have indicated that GLYATL1 may also be implicated in the regulation of energy homeostasis and oxidative stress responses, making it a potential target for therapeutic interventions. Additionally, recombinant GLYATL1 protein has emerged as a valuable tool for elucidating the enzyme's structure-function relationships and substrate specificity. Through the expression and purification of recombinant GLYATL1, researchers can conduct in vitro assays to investigate its enzymatic activity, interaction with substrates, and response to inhibitors. This research is crucial for identifying the biochemical pathways involving GLYATL1, ultimately contributing to the development of strategies to manage conditions linked to glycine metabolism dysregulation. Understanding the molecular mechanisms of GLYATL1 will inform future studies aimed at exploring its potential roles in health and disease.
