Analytical Data
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Gene name
GLYATL2
- Application
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Alternative Names
GLYATL2GAT;Glycine N-acyltransferase-like Protein 2
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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
Q8WU03
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Expression Region
1-294aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMLVLHNSQKLQILYKSLEKSIPESIKV YGAIFNIKDKNPFNMEVLVDAWPDYQIVITRPQKQEMKDDQDHYTNTYHI FTKAPDKLEEVLSYSNVISWEQTLQIQGCQEGLDEAIRKVATSKSVQVDY MKTILFIPELPKKHKTSSNDKMELFEVDDDNKEGNFSNMFLDASHAGLVN EHWAFGKNERSLKYIERCLQDFLGFGVLGPEGQLVSWIVMEQSCELRMGY TVPKYRHQGNMLQIGYHLEKYLSQKEIPFYFHVADNNEKSLQALNNLGFK ICPCGWHQWKCTPKKYC
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Molecular Weight
37 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
GLYATL2, a member of the glycine N-methyltransferase family, has garnered significant interest in biomedical research due to its potential role in regulating glycine metabolism and associated pathways. Glycine, an amino acid, is crucial for various physiological processes, including protein synthesis and neurotransmission. Dysregulation of glycine levels has been linked to several health conditions, including neurological disorders and metabolic syndromes. Studying the recombinant GLYATL2 protein enables researchers to elucidate its enzymatic properties, substrate specificity, and interaction with other metabolites. Additionally, understanding GLYATL2’s function can provide insights into its involvement in critical cellular processes and its potential as a therapeutic target for diseases linked to glycine dysregulation. This research also contributes to the broader understanding of methylation processes in human health and disease, highlighting the importance of GLYATL2 in metabolic pathways and its potential implications for drug development and clinical applications. Overall, the exploration of GLYATL2's recombinant protein adds a significant dimension to our understanding of metabolic enzymes and their roles in maintaining homeostasis.
