HPA012628

Sigma-Aldrich

Anti-GALNT1 antibody produced in rabbit

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

Synonym(s):
Anti-Polypeptide GalNAc transferase 1, Anti-UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, Anti-Polypeptide N-acetylgalactosaminyltransferase 1, Anti-Protein-UDP acetylgalactosaminyltransferase 1, Anti-GalNAc-T1, Anti-pp-GaNTase 1
Human Protein Atlas Number:

biological source

rabbit

Quality Level

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

packaging

antibody small pack of 25 μL

application(s)

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:50-1:200

immunogen sequence

KERGLPAGDVLEPVQKPHEGPGEMGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPD

conjugate

unconjugated

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... GALNT1(2589)

Related Categories

General description

Polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) is localized to the Golgi apparatus. The gene encoding this protein is present on chromosome 18q12-q21.

Immunogen

polypeptide N-acetylgalactosaminyltransferase 1

Biochem/physiol Actions

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.

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 APREST72011.

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 Sigma-Aldrich Co. LLC

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.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

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....
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...
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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