Analytical Data
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Gene name
DPM3
- Application
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Alternative Names
DPM3; Dolichol-phosphate mannosyltransferase subunit 3; Dolichol-phosphate mannose synthase subunit 3; DPM synthase subunit 3; Dolichyl-phosphate beta-D-mannosyltransferase subunit 3
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9P2X0
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Expression Region
1-122aa
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AA Sequence
MLSVGGLRLSLVRFSFLLLRGALLPSLAVTMTKLAQWLWGLAILGSTWVALTTGALGLELPLSCQEVLWPLPAYLLVSAGCYALGTVGYRVATFHDCEDAARELQSQIQEARADLARRGLRF
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Molecular Weight
39.7 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
DPM3 (Dolichyl-phosphate mannose synthase subunit 3) is a crucial protein involved in the biosynthesis of N-glycans, which are essential for the proper folding and stability of glycoproteins. Research on DPM3 has gained significant attention due to its role in various cellular processes and its implications in human health. Mutations in the DPM3 gene can lead to a rare genetic disorder known as Congenital Disorders of Glycosylation (CDG), characterized by a range of developmental and neurological abnormalities. Consequently, understanding the structure, function, and regulation of DPM3 is essential for developing potential therapeutic approaches for conditions linked to glycosylation defects. Furthermore, studies on DPM3 have provided insights into the broader mechanisms of glycoprotein synthesis, contributing to the fields of glycobiology and biotechnology. Recombination techniques have enabled researchers to produce DPM3 protein in laboratory settings, facilitating in-depth functional studies. Overall, the investigation of DPM3 and its associated pathways is vital for unraveling the complexities of glycosylation and its impact on health and disease.
