Analytical Data
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Gene name
MGAT2
- Application
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Alternative Names
MGAT2;Alpha-1.6-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
Q10469
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Expression Region
30-447aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MRQRKNEALA PPLLDAEPAR GAGGRGGDHP SVAVGIRRVS NVSAASLVPA VPQPEADNLT LRYRSLVYQL NFDQTLRNVD KAGTWAPREL VLVVQVHNRP EYLRLLLDSL RKAQGIDNVL VIFSHDFWST EINQLIAGVN FCPVLQVFFP FSIQLYPNEF PGSDPRDCPR DLPKNAALKL GCINAEYPDS FGHYREAKFS QTKHHWWWKL HFVWERVKIL RDYAGLILFL EEDHYLAPDF YHVFKKMWKL KQQECPECDV LSLGTYSASR SFYGMADKVD VKTWKSTEHN MGLALTRNAY QKLIECTDTF CTYDDYNWDW TLQYLTVSCL PKFWKVLVPQ IPRIFHAGDC GMHHKKTCRP STQSAQIESL LNNNKQYMFP ETLTISEKFT VVAISPPRKN GGWGDIRDHE LCKSYRRLQ
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Molecular Weight
50 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
MGAT2, or Mannosyltransferase 2, is a member of the glycosyltransferase family that plays a crucial role in glycosylation processes, specifically in the synthesis of complex N-glycans. These glycans are essential for various biological functions, including cell signaling, immune response, and protein stability. Research on MGAT2 has gained significance due to its involvement in various diseases, including cancer and metabolic disorders, where altered glycosylation patterns can influence disease progression and patient outcomes. Understanding the structure and function of MGAT2 can provide insights into its catalytic mechanism and the regulation of glycosylation pathways. Additionally, recombinant MGAT2 proteins have potential applications in biotechnology, such as in the manufacture of therapeutic glycoproteins. Recent studies have focused on expressing MGAT2 in heterologous systems to produce active enzyme for biochemical assays and structural studies. These investigations aim to elucidate the enzyme's substrate specificity, kinetic parameters, and potential inhibitors, thereby contributing to the development of targeted therapies that leverage glycosylation manipulation. Overall, the study of MGAT2 recombinant proteins is pivotal in advancing our understanding of glycosylation biology and its implications in health and disease.
