Analytical Data
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Gene name
GLYAT
- Application
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Alternative Names
GLYAT；ACGNAT；CAT;Glycine N-acyltransferase
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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
Q6IB77
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Expression Region
1-296aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMMLPLQGAQMLQMLEKSLRKSLPASLKVYG TVFHINHGNPFNLKAVVDKWPDFNTVVVCPQEQDMTDDLDHYTNTYQIYS KDPQNCQEFLGSPELINWKQHLQIQSSQPSLNEAIQNLAAIKSFKVKQTQ RILYMAAETAKELTPFLLKSKILSPSGGKPKAINQEMFKLSSMDVTHAHL VNKFWHFGGNERSQRFIERCIQTFPTCCLLGPEGTPVCWDLMDQTGEMRM AGTLPEYRLHGLVTYVIYSHAQKLGKLGFPVYSHVDYSNEAMQKMSYTLQ HVPIPRSWNQWNCVPL
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Molecular Weight
36 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
GLYAT, or glycine N-acyltransferase, is an important enzyme involved in the metabolism of glycine and the detoxification of various acyl-CoA derivatives. Research into GLYAT has gained prominence due to its role in metabolic pathways, particularly in the context of amino acid conjugation and the regulation of biochemical processes. Abnormalities in GLYAT function have been linked to various metabolic disorders, highlighting its potential as a therapeutic target. The recombinant production of GLYAT protein has enabled detailed studies into its enzymatic properties, substrate specificity, and regulatory mechanisms. Furthermore, understanding the structure-function relationship of GLYAT can provide insights into its role in health and disease. The development of recombinant GLYAT not only facilitates the exploration of its biochemical properties but also opens avenues for drug development and the design of therapeutic strategies for conditions linked to glycine metabolism dysregulation. As such, ongoing research into GLYAT, including its recombinant protein forms, is critical for advancing our knowledge of metabolic regulation and its implications in human health.
