HPA012628
Anti-GALNT1 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Sinónimos:
Anti-GalNAc-T1, Anti-Polypeptide GalNAc transferase 1, Anti-Polypeptide N-acetylgalactosaminyltransferase 1, Anti-Protein-UDP acetylgalactosaminyltransferase 1, Anti-UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, Anti-pp-GaNTase 1
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About This Item
Productos recomendados
origen biológico
rabbit
conjugado
unconjugated
forma del anticuerpo
affinity isolated antibody
tipo de anticuerpo
primary antibodies
clon
polyclonal
Línea del producto
Prestige Antibodies® Powered by Atlas Antibodies
formulario
buffered aqueous glycerol solution
reactividad de especies
human
técnicas
immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:50-1:200
secuencia del inmunógeno
KERGLPAGDVLEPVQKPHEGPGEMGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPD
Nº de acceso UniProt
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
modificación del objetivo postraduccional
unmodified
Información sobre el gen
human ... GALNT1(2589)
Categorías relacionadas
Descripción general
Polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) is localized to the Golgi apparatus. The gene encoding this protein is present on chromosome 18q12-q21.
Inmunógeno
polypeptide N-acetylgalactosaminyltransferase 1
Aplicación
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.
Acciones bioquímicas o fisiológicas
Polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) is involved in catalyzing the initial reaction of O-linked oligosaccharide biosynthesis. It has a wide range of protein substrates. GALNT1 transfers an N-acetyl-D-galactosamine residue to a serine or threonine residue which is present on the protein substrate.
Características y beneficios
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.
Ligadura / enlace
Corresponding Antigen APREST72011
Forma física
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Información legal
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Cláusula de descargo de responsabilidad
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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Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
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
S Röttger et al.
Journal of cell science, 111 ( Pt 1), 45-60 (1998-02-28)
O-glycosylation of proteins is initiated by a family of UDP-N-acetylgalactosamine:polypeptide N-acetylgalactos-aminyltransferases (GalNAc-T). In this study, we have localized endogenous and epitope-tagged human GalNAc-T1, -T2 and -T3 to the Golgi apparatus in HeLa cells by subcellular fractionation, immunofluorescence and immunoelectron microscopy.
Shengjun Wang et al.
Nature communications, 15(1), 4162-4162 (2024-05-17)
The multibasic furin cleavage site at the S1/S2 boundary of the spike protein is a hallmark of SARS-CoV-2 and plays a crucial role in viral infection. However, the mechanism underlying furin activation and its regulation remain poorly understood. Here, we
E P Bennett et al.
Glycobiology, 8(6), 547-555 (1998-06-11)
A homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here
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