Analytical Data
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Gene name
GLYATL1
- Application
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Alternative Names
GLYATL1；GNAT；Glycine N-acyltransferase-like Protein 1
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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
Q969I3
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Expression Region
1-302aa
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AA Sequence
MILLNNSHKLLALYKSLARSIPESLKVYGSVYHINHGNPFNMEVLVDSWPEYQMVIIRPQKQEMTDDMDSYTNVYRMFSKEPQKSEEVLKNCEIVNWKQRLQIQGLQESLGEGIRVATFSKSVKVEHSRALLLVTEDILKLNASSKSKLGSWAETGHPDDEFESETPNFKYAQLDVSYSGLVNDNWKRGKNERSLHYIKRCIEDLPAACMLGPEGVPVSWVTMDPSCEVGMAYSMEKYRRTGNMARVMVRYMKYLRQKNIPFYISVLEENEDSRRFVGQFGFFEASCEWHQWTCYPQNLVPF
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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 significant role in the metabolism of amino acids and the synthesis of glycine-conjugated metabolites. Understanding the function and regulation of GLYATL1 is crucial, as it has been implicated in several physiological processes, including neurotransmission and the detoxification of xenobiotics. Recent studies have suggested that GLYATL1 may also be involved in various diseases, including metabolic disorders and neurodegenerative diseases, making it a potential therapeutic target. However, the detailed mechanisms of its action and the structural properties of GLYATL1 remain largely underexplored. The development of recombinant GLYATL1 protein is essential for characterizing its enzymatic activities, understanding its interaction with substrates, and elucidating its role in biological systems. By producing this protein through recombinant methods, researchers can investigate its properties using biochemical assays, biophysical techniques, and structural biology approaches. Moreover, studying GLYATL1 in a recombinant context allows for the examination of its potential as a biomarker or drug target, paving the way for novel therapeutic strategies. Overall, the research on recombinant GLYATL1 protein is aimed at filling the knowledge gap surrounding its biological function and its implications in health and disease.
