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Merck
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安全信息

HPA007613

Sigma-Aldrich

Anti-GALNT3 antibody produced in rabbit

enhanced validation

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

别名:

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

UNSPSC代码:
12352203
人类蛋白质图谱编号:
NACRES:
NA.41

生物来源

rabbit

质量水平

偶联物

unconjugated

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

产品线

Prestige Antibodies® Powered by Atlas Antibodies

形式

buffered aqueous glycerol solution

种属反应性

human

增强验证

orthogonal RNAseq
Learn more about Antibody Enhanced Validation

技术

immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500

免疫原序列

EESRMERNMKNKNKMLDLMLEAVNNIKDAMPKMQIGAPVRQNIDAGERPCLQGYYTAAELKPVLDRPPQDSNAPGASGKAFKTTNLSVEEQKEKERGEAKHC

UniProt登记号

运输

wet ice

储存温度

−20°C

靶向翻译后修饰

unmodified

基因信息

human ... GALNT3(2591)

一般描述

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.

免疫原

polypeptide N-acetylgalactosaminyltransferase 3

应用

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.

生化/生理作用

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.

特点和优势

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.

联系

Corresponding Antigen APREST71818

外形

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

法律信息

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

免责声明

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

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

法规信息

常规特殊物品

分析证书(COA)

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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
S Kitada et al.
British journal of cancer, 109(2), 472-481 (2013-06-27)
The polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts) family of enzymes regulates the initial steps of mucin-type O-glycosylation. N-acetylgalactosaminyltransferases might show novel patterns of GalNAc-T glycosylation on tumour-derived proteins, which could influence cancer biology, but its mechanisms are unclear. We investigated the association of
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
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
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.

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