Analytical Data
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Gene name
GNMT
- Application
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Alternative Names
GNMT;Glycine N-methyltransferase
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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
Q14749
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Expression Region
2-295aa
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AA Sequence
VDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD
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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
The research background of GNMT (Glycine N-Methyltransferase) recombinant protein centers on its critical role in methylation processes and amino acid metabolism. GNMT is an enzyme that catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine, producing sarcosine and S-adenosylhomocysteine. This reaction is essential for regulating glycine levels in the body and maintaining proper metabolic functions. Dysregulation of GNMT has been implicated in various health issues, including liver diseases, obesity, and neurological disorders, making it a significant target for therapeutic intervention. The production of recombinant GNMT facilitates detailed studies into its structure, function, and interactions within metabolic pathways. Furthermore, understanding GNMT's enzymatic mechanisms can lead to developing drugs that modulate its activity, offering potential treatments for conditions linked to its dysfunction. As such, the investigation of GNMT recombinant protein is vital for expanding our knowledge of metabolic regulation and exploring novel biomedical applications.
