Analytical Data
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Gene name
PMT2
- Application
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Species
Saccharomyces cerevisiae
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P31382
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Expression Region
311-609aa
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Molecular Weight
38.0 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
PMT2, a crucial enzyme in the biosynthetic pathway of protein modification, has attracted considerable attention in biochemical research due to its role in the post-translational modification of proteins. This enzyme is known to catalyze the transfer of mannose residues to target proteins, a process vital for their proper folding, stability, and function. Research on PMT2 is particularly significant as defects in protein glycosylation are linked to various diseases, including cancer and genetic disorders. Understanding the structure and function of PMT2 can provide insights into the mechanisms of glycoprotein synthesis, potentially leading to the development of therapeutic strategies for related diseases. Moreover, the study of PMT2 and its interactions with other cellular components could elucidate the broader implications of glycosylation on cell signaling and immune responses. Recent advances in structural biology have enabled detailed investigations of PMT2, paving the way for the engineering of this enzyme for biotechnological applications. Given its pivotal role in modifying proteins, PMT2 serves as an ideal candidate for studies aimed at improving the efficiency and specificity of glycosylation in recombinant proteins, which is particularly relevant in the fields of biopharmaceuticals and synthetic biology. Overall, continuing research into PMT2 not only enhances our understanding of glycosylation processes but also holds promise for innovative solutions in medical and industrial biotechnology.
