Analytical Data
-
Gene name
ENGASE
- Application
-
Alternative Names
ENGASE；Cytosolic endo-beta-N-acetylglucosaminidase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8NFI3
-
Expression Region
1-377aa
-
AA Sequence
MEAAAVTVTRSATRRRRRQLQGLAAPEAGTQEEQEDQEPRPRRRRPGRSIKDEEEETVFREVVSFSPDPLPVRYYDKDTTKPISFYLSSLEELLAWKPRLEDGFNVALEPLACRQPPLSSQRPRTLLCHDMMGGYLDDRFIQGSVVQTPYAFYHWQCIDVFVYFSHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNEGGRLCEAFLAGDERSYQAVADRLVQITQFFRFDGWLINIENSLSLAAVGNMPPFLRYLTTQLHRQVPGGLVLWYDSVVQSGQLKWQDELNQHNRVFFDSCDGFFTNYNWREEHLERMLGQAGERRADVYVGVDVFARGNVVGGRFDTDKSLELIRKHGFSVALFAPSCSVFPGVGNLLCC
-
Molecular Weight
59.1 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
ENGASE (Endoglycosidase) is a specialized enzyme that plays a crucial role in the processing of glycoproteins, making it significant in various biotechnological and therapeutic applications. The understanding of ENGASE's function has gained prominence due to its ability to cleave specific glycan structures from glycoproteins, thereby facilitating the study of protein folding, stability, and interactions. Research in this field has focused on the enzyme's potential for use in diagnostic tools, the enhancement of recombinant protein production, and the development of novel biopharmaceuticals. ENGASE has been increasingly recognized for its importance in the study of glycosylation, a critical post-translational modification that impacts protein functionality. Advances in biotechnology have enabled the expression and purification of ENGASE from different sources, allowing for detailed investigations into its enzymatic mechanisms and substrate specificity. Insights gained from these studies are paving the way for innovative therapeutic strategies, particularly in the treatment of diseases linked to glycosylation anomalies, such as congenital disorders of glycosylation and certain types of cancer. As research progresses, the exploration of ENGASE's structural and functional properties continues to unveil new possibilities for its application in glycoprotein engineering and therapeutic interventions, underscoring its significance in the field of glycobiology and biomedicine.
