Analytical Data
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Gene name
GATM
- Application
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Alternative Names
GATM；AGAT;Glycine amidinotransferase. mitochondrial
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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
P50440
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Expression Region
38-423aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMSTQAATASSRNSCAADDKATEPLPKD CPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGH YFPKDHLKKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGL YSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTA PKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGR DIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGP GIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVL MLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVR RRGTLQSYLD
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Molecular Weight
47 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
GATM, or Glycine Amidotransferase, is an enzyme crucial for the synthesis of glycine, an important amino acid that plays a key role in various metabolic processes, including neurotransmitter regulation and the synthesis of proteins. Research on GATM has gained traction due to its potential implications in various health conditions, particularly in the context of metabolic disorders and neurological diseases. Alterations in glycine levels have been linked to conditions such as schizophrenia and non-alcoholic fatty liver disease, making the study of GATM particularly relevant for understanding these pathologies. Additionally, the investigation of GATM in the context of therapeutic interventions has emerged, aiming to modulate its activity to restore normal glycine levels. The recombinant production of GATM protein has opened avenues for detailed studies of its structure-function relationships, allowing researchers to explore the enzyme's mechanisms and its interactions with co-factors and substrates. Understanding these aspects can contribute significantly to the development of specific inhibitors or enhancers of GATM activity, which could lead to novel treatment strategies for diseases associated with glycine dysregulation. Thus, GATM represents not only a pivotal enzyme in amino acid metabolism but also a promising target for medical research aimed at addressing several significant health challenges.
