Analytical Data
-
Gene name
DHDDS
- Application
-
Alternative Names
DHDDS；HDS；Dehydrodolichyl diphosphate synthase complex subunit DHDDS
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q86SQ9
-
Expression Region
1-333aa
-
AA Sequence
MSWIKEGELSLWERFCANIIKAGPMPKHIAFIMDGNRRYAKKCQVERQEGHSQGFNKLAETLRWCLNLGILEVTVYAFSIENFKRSKSEVDGLMDLARQKFSRLMEEKEKLQKHGVCIRVLGDLHLLPLDLQELIAQAVQATKNYNKCFLNVCFAYTSRHEISNAVREMAWGVEQGLLDPSDISESLLDKCLYTNRSPHPDILIRTSGEVRLSDFLLWQTSHSCLVFQPVLWPEYTFWNLFEAILQFQMNHSVLQKARDMYAEERKRQQLERDQATVTEQLLREGLQASGDAQLRRTRLHKLSARREERVQGFLQALELKRADWLARLGTASA
-
Molecular Weight
65.7 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
DHDDS (Dolichyl-phosphate β-D-mannosyltransferase) is an essential enzyme involved in the biosynthesis of N-glycans, crucial for proper protein folding and cell signaling. Its primary function is to transfer mannose residues from dolichyl phosphate mannose (DPM) to the growing oligosaccharide chain during N-glycosylation, a critical post-translational modification. Dysregulation of DHDDS activity has been linked to various diseases, including congenital disorders of glycosylation, which can lead to severe neurological and developmental issues. As such, understanding the structure and function of DHDDS is vital for deciphering the complexities of glycosylation pathways and their implications in human health. Recent advancements in recombinant protein technology have enabled researchers to produce DHDDS in sufficient quantities for detailed biochemical characterization and structural studies, facilitating insights into its catalytic mechanism and regulation. This research is not only pivotal for uncovering the roles of glycosylation in cellular processes but also for developing therapeutic strategies aimed at correcting glycosylation defects.
