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Key Documents

HPA001141

Sigma-Aldrich

Anti-A4GALT antibody produced in rabbit

affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-α-1,4-Galactosyltransferase antibody produced in rabbit, Anti-α-1,4-N-Acetylglucosaminyltransferase antibody produced in rabbit, Anti-α4Gal-T1 antibody produced in rabbit, Anti-Lactosylceramide 4-(α-galactosyltransferase) antibody produced in rabbit, Anti-UDP-galactose:β-D-galactosyl-β1-R 4-(α-D-galactosyltransferase) antibody produced in rabbit

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.43

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

human

technique(s)

immunofluorescence: 0.25-2 μg/mL

immunogen sequence

WEPYLLPVLSDASRIALMWKFGGIYLDTDFIVLKNLRNLTNVLGTQSRYVLNGAFLAFERRHEFMALCMRDFVDHYNGWIWGHQGPQLLTRVFKKWCSIRSLAESRACRGVTTLPPEAFYPIPWQDWKKYFEDINPEELPRLLSATYAVH

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... A4GALT(53947)

General description

The gene A4GALT (α 1,4-galactosyltransferase) is mapped to human chromosome 22q13.2.

Immunogen

Lactosylceramide 4-(α-galactosyltransferase) 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

Lactosylceramide 4-α-galactosyltransferase is an enzyme encoded by the A4GALT gene in humans. It plays a very crucial role for P1 and P(k) synthesis of the P blood group system. This gene may help in improving genetic blood group prediction. Alteration in the structural gene causes Fabry disease (it is a treatable X-linked lysosomal storage disorder). It may also be associated with cardiovascular and/or kidney disease and decreased life span.

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 APREST73401

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Julia S Westman et al.
Transfusion, 54(7), 1831-1835 (2014-01-15)
Cells of the clinically important p histo-blood group phenotype lack P1, P(k) , and P glycosphingolipid antigens. All cases investigated so far are due to alterations in the 4-α-galactosyltransferase-encoding Exon 3 of A4GALT. Repetitive elements in the genome can mediate
Britt Thuresson et al.
Blood, 117(2), 678-687 (2010-10-26)
The A4GALT locus encodes a glycosyltransferase that synthesizes the terminal Galα1-4Gal of the P(k) (Gb3/CD77) glycosphingolipid, important in transfusion medicine, obstetrics, and pathogen susceptibility. Critical nucleotide changes in A4GALT not only abolish P(k) formation but also another Galα1-4Gal-defined antigen, P1
Eduard Paschke et al.
American journal of kidney diseases : the official journal of the National Kidney Foundation, 57(5), 673-681 (2010-12-28)
Fabry disease is a treatable X-linked lysosomal storage disorder caused by alterations in the structural gene (GLA) of α-galactosidase A (AGAL), manifesting with cardiovascular and/or kidney disease and decreased life span. Although males as well as females can be affected
Kyle P Heim et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(44), 15746-15751 (2014-10-22)
The cariogenic bacterium Streptococcus mutans uses adhesin P1 to adhere to tooth surfaces, extracellular matrix components, and other bacteria. A composite model of P1 based on partial crystal structures revealed an unusual complex architecture in which the protein forms an

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