Analytical Data
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Gene name
GNTI
- Application
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Alternative Names
GNTI；CGL1；Alpha-1.3-mannosyl-glycoProtein 2-beta-N-acetylglucosaminyltransferase
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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
Q9XGM8
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Expression Region
25-444aa
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AA Sequence
RLFQTQSQYADRLSSAIESENHCTSQMRGLIDEVSIKQSRIVALEDMKNRQDEELVQLKDLIQTFEKKGIAKLTQGGQMPVAAVVVMACSRADYLERTVKSVLTYQTPVASKYPLFISQDGSDQAVKSKSLSYNQLTYMQHLDFEPVVTERPGELTAYYKIARHYKWALDQLFYKHKFSRVIILEDDMEIAPDFFDYFEAAASLMDRDKTIMAASSWNDNGQKQFVHDPYALYRSDFFPGLGWMLKRSTWDELSPKWPKAYWDDWLRLKENHKGRQFIRPEVCRTYNFGEHGSSLGQFFSQYLEPIKLNDVTVDWKAKDLGYLTEGNYTKYFSGLVRQARPIQGSDLVLKAQNIKDDVRIRYKDQVEFERIAGEFGIFEEWKDGVPRTAYKGVVVFRIQTTRRVFLVGPDSVMQLGIRNS
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Molecular Weight
51.6 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
GNTI, or Glycerol-3-phosphate acyltransferase, is an enzyme implicated in the regulation of lipid metabolism and synthesis in various biological systems. Research on GNTI has gained momentum due to its potential role in influencing cellular energy homeostasis and membrane dynamics. Disruptions in lipid metabolism are linked to several metabolic disorders, including obesity, diabetes, and cardiovascular diseases, underscoring the need for a deeper understanding of GNTI's functions and mechanisms. Moreover, GNTI is of interest in the field of biochemistry and molecular biology for its involvement in phospholipid biosynthesis pathways, which are crucial for cell membrane integrity and signaling. Investigating the structural and functional aspects of GNTI, particularly through recombinant protein studies, allows scientists to explore its catalytic mechanisms and regulatory mechanisms in detail. This research not only advances our understanding of fundamental biological processes but also opens avenues for developing therapeutic strategies targeting lipid-related disorders. Overall, the study of GNTI and its recombinant protein form is pivotal in bridging gaps in our current knowledge of lipid metabolism and its implications for human health.
