Analytical Data
-
Gene name
PMT5
- Application
-
Alternative Names
PMT5; YDL093W; D2399; Dolichyl-phosphate-mannose--protein mannosyltransferase 5; EC 2.4.1.109
-
Species
Saccharomyces cerevisiae
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P52867
-
Expression Region
286-583aa
-
Molecular Weight
38.6 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
PMT5 (Protein O-mannosyltransferase 5) is an enzyme that plays a critical role in the glycosylation process of proteins in various organisms, including yeast and mammals. Its primary function is to transfer mannose moieties to specific serine or threonine residues on target proteins, a modification that is essential for proper protein folding, stability, and biological activity. Research on PMT5 is particularly significant because defects in protein O-mannosylation are linked to various diseases, including certain congenital disorders and neurodegenerative diseases. Understanding the structure and function of PMT5 can provide insights into its role in cellular processes and its potential implications in disease pathology. Advances in recombinant protein technology have allowed for the production of functional PMT5 in sufficient quantities, enabling detailed studies of its enzymatic mechanisms and substrate specificity. Additionally, characterizing PMT5 could lead to the development of therapeutic strategies aimed at correcting glycosylation defects, thereby enhancing our overall understanding of protein post-translational modifications. As a result, the ongoing research on PMT5 is not only crucial for basic biological science but also has promising applications in biotechnology and medicine, making it a focal point of investigation in the broader field of glycobiology.
