HPA007613
Anti-GALNT3 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonim(y):
Anti-GalNAc-T3 antibody produced in rabbit, Anti-Polypeptide GalNAc transferase 3 antibody produced in rabbit, Anti-Polypeptide N-acetylgalactosaminyltransferase 3 antibody produced in rabbit, Anti-Protein-UDP acetylgalactosaminyltransferase 3 antibody produced in rabbit, Anti-UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 antibody produced in rabbit, Anti-pp-GaNTase 3 antibody produced in rabbit
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About This Item
pochodzenie biologiczne
rabbit
Poziom jakości
białko sprzężone
unconjugated
forma przeciwciała
affinity isolated antibody
rodzaj przeciwciała
primary antibodies
klon
polyclonal
linia produktu
Prestige Antibodies® Powered by Atlas Antibodies
Postać
buffered aqueous glycerol solution
reaktywność gatunkowa
human
rozszerzona walidacja
orthogonal RNAseq
Learn more about Antibody Enhanced Validation
metody
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500
sekwencja immunogenna
EESRMERNMKNKNKMLDLMLEAVNNIKDAMPKMQIGAPVRQNIDAGERPCLQGYYTAAELKPVLDRPPQDSNAPGASGKAFKTTNLSVEEQKEKERGEAKHC
numer dostępu UniProt
Warunki transportu
wet ice
temp. przechowywania
−20°C
docelowa modyfikacja potranslacyjna
unmodified
informacje o genach
human ... GALNT3(2591)
Powiązane kategorie
Opis ogólny
GALNT3 (polypeptide N-acetylgalactosaminyltransferase 3) is a cell adhesion molecule belonging to the polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts) family. It is majorly involved in the regulation of initial steps of mucin-type O-glycosylation.
Immunogen
polypeptide N-acetylgalactosaminyltransferase 3
Zastosowanie
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.
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.
Działania biochem./fizjol.
GALNT3 (polypeptide N-acetylgalactosaminyltransferase 3) gene encoded proteins catalyze the transfer of GalNAc from UDP-GalNAc to either serine or threonine residues of polypeptide acceptors. GALNT3 catalyzes the initiation of O-linked oligosaccharide biosynthesis. Protein glycosylation of target proteins is important in stabilizing the half-life, biological activity and receptor recognition of these proteins. Defects in this gene have been associated with rare autosomal recessive metabolic disorder familial tumoral calcinosis characterized by hyperphosphatemia and massive ectopic calcifications.
Cechy i korzyści
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:
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.
Powiązanie
Corresponding Antigen APREST71818
Postać fizyczna
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Informacje prawne
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Oświadczenie o zrzeczeniu się odpowiedzialności
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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Kod klasy składowania
10 - Combustible liquids
Klasa zagrożenia wodnego (WGK)
WGK 1
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Środki ochrony indywidualnej
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certyfikaty analizy (CoA)
Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.
Masz już ten produkt?
Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
E P Bennett et al.
The Journal of biological chemistry, 271(29), 17006-17012 (1996-07-19)
The glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report
Kentaro Kato et al.
The Journal of biological chemistry, 281(27), 18370-18377 (2006-04-28)
Mutations in the gene encoding the glycosyltransferase polypeptide GalNAc-T3, which is involved in initiation of O-glycosylation, were recently identified as a cause of the rare autosomal recessive metabolic disorder familial tumoral calcinosis (OMIM 211900). Familial tumoral calcinosis is associated with
Romina B Cejas et al.
The Journal of biological chemistry, 294(9), 2997-3011 (2018-12-29)
Biological functions of nuclear proteins are regulated by post-translational modifications (PTMs) that modulate gene expression and cellular physiology. However, the role of O-linked glycosylation (O-GalNAc) as a PTM of nuclear proteins in the human cell has not been previously reported.
H H Wandall et al.
The Journal of biological chemistry, 272(38), 23503-23514 (1997-09-20)
Mucin-type O-glycosylation is initiated by UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). The role each GalNAc-transferase plays in O-glycosylation is unclear. In this report we characterized the specificity and kinetic properties of three purified recombinant GalNAc-transferases. GalNAc-T1, -T2, and -T3 were expressed as soluble
Virginia Lorenz et al.
The Journal of biological chemistry, 291(49), 25339-25350 (2016-10-16)
Glycan biosynthesis occurs mainly in Golgi. Molecular organization and functional regulation of this process are not well understood. We evaluated the extrinsic effect of lectin domains (β-trefoil fold) of polypeptide GalNAc-transferases (ppGalNAc-Ts) on catalytic activity of glycosyltransferases during O-GalNAc glycan
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