Description
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, 2 bp deletion in exon 2 and 4 bp deletion in exon 2,
Disease:Adenocarcinoma
Product details:
We will provide viable cells that proliferate on revival.
This product is subject to limited use licenses from The Broad Institute and ERS Genomics Limited, and is developed with patented technology. For full details of the limited use licenses and relevant patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-DPM2, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--196°C, Appropriate long-term storage conditions--196°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
DPM2 also known as dolichyl-phosphate mannosyltransferase polypeptide 2 is a component of the dolichol-phosphate mannose (DPM) synthase complex. This protein weighs approximately 25 kDa and plays a significant role in mannose transfer. It is ubiquitously expressed in various tissues with higher expression levels in the liver heart and muscle. The DPM2 works as a regulator and stabilizer within the DPM synthase complex essential for glycosylation processes.
Biological function summary
DPM2 is involved in the assembly of the glycosylation precursor dolichol-phosphate-mannose which is critical for the proper synthesis of glycoproteins. As part of the DPM synthase complex DPM2 teams with the catalytic subunit DPM1 and the anchoring subunit DPM3. These interactions ensure effective glycosylation necessary for protein folding and function. The glycosylation process is essential for the stability and activity of numerous proteins within eukaryotic organisms.
Pathways
DPM2 plays a central role in the protein glycosylation pathway and the synthesis of glycosylphosphatidylinositol (GPI) anchors. It works closely with DPM1 activating it to transfer mannose molecules from GDP-mannose to dolichol-phosphate an important step in the formation of GPI-anchored proteins. These pathways are vital for cell surface expression and protein localization implicating DPM2 in broader cell signaling and communication networks.
DPM2 mutations are linked to Congenital Disorders of Glycosylation (CDG) particularly CDG-Iu. These conditions affect multiple systems due to improper glycosylation leading to symptoms ranging from developmental delays to organ dysfunction. Furthermore DPM2 in association with DPM1 and other partners in the DPM synthase complex has connections to muscular dystrophies due to its role in muscle glycosylation processes. Understanding these relationships is important for developing therapeutic interventions targeting glycosylation-related disorders.
