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HPA014667

Sigma-Aldrich

Anti-DPM3 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-DPM synthase complex subunit 3, Anti-Dolichol-phosphate mannose synthase subunit 3, Anti-Dolichol-phosphate mannosyltransferase subunit 3, Anti-Dolichyl-phosphate beta-D-mannosyltransferase subunit 3, Anti-MPD synthase subunit 3, Anti-Mannose-P-dolichol synthase subunit 3

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:20-1:50

immunogen sequence

FHDCEDAARELQSQIQEARADLARR

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DPM3(54344)

General description

DPM3 (dolichyl-phosphate mannosyltransferase polypeptide 3) is a component of dolichol-P-mannose (Dol-P-Man or DPM) synthase complex, which also includes DPM1 and DPM2. It is a transmembrane protein, which resides in the endoplasmic reticulum (ER). It has two alternatively spliced isoforms, which differ in the length of their N-termini. Its transmembrane region is present in the N-terminal, and the C-terminal is hydrophilic in nature, and binds to DPM1. It is composed of 92 amino acids, and has a coiled-coil domain in its C-terminal.

Immunogen

Dolichol-phosphate mannosyltransferase subunit 3 recombinant protein epitope signature tag (PrEST)

Application

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Biochem/physiol Actions

DPM3 (dolichyl-phosphate mannosyltransferase polypeptide 3) anchors the cytosolic catalytic subunit DPM1 to the endoplasmic reticulum (ER) membrane, in the DPM complex. This complex catalyzes the conversion of GDP-mannose and dolichol-phosphate to dolichol-P-mannose. Mutation in this gene, in one female patient, was found to be linked to congenital disorders of glycosylation (CDG) type I, characterized by mild muscular dystrophy, dilated cardiomyopathy and increased levels of transaminases. Its expression is regulated by PLC (phospholipase C)γ, and it responds to androgen in non-invasive prostate cancer cells. It suppresses prostate cancer invasiveness, and promotes cell apoptosis. It might also be involved in maintaining normal cell-extracellular matrix (ECM) interactions, by regulating the normal expression of GPI-linked cell surface proteins. Mutations in this gene result in α-dystroglycanopathy, and thus, this protein acts as a link between α-dystroglycanopathy and CDG.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST72976

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Amy C Yang et al.
Molecular genetics and metabolism, 110(3), 345-351 (2013-07-17)
Congenital disorders of glycosylation (CDG) are rare genetic defects mainly in the post-translational modification of proteins via attachment of carbohydrate chains. We describe an infant with the phenotype of a congenital muscular dystrophy, with borderline microcephaly, hypotonia, camptodactyly, severe motor
Hisashi Ashida et al.
The Journal of biological chemistry, 281(2), 896-904 (2005-11-11)
Dolichol-phosphate mannose (DPM) synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. We previously identified DPM3, the third component of this enzyme, which was co-purified with DPM1 and DPM2. Here, we have established
E J Manos et al.
Oncogene, 20(22), 2781-2790 (2001-06-23)
The most ominous development in tumor progression is the transition to an invasive and metastatic phenotype. Little is known, however, about the molecular alterations that cause a tumor to become invasive. In view of this, we have used microarray expression
Dirk J Lefeber et al.
American journal of human genetics, 85(1), 76-86 (2009-07-07)
Alpha-dystroglycanopathies such as Walker Warburg syndrome represent an important subgroup of the muscular dystrophies that have been related to defective O-mannosylation of alpha-dystroglycan. In many patients, the underlying genetic etiology remains unsolved. Isolated muscular dystrophy has not been described in

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