SAB3500988
Anti-GALNT10 antibody produced in rabbit
affinity isolated antibody
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
mouse, human, rat
concentration
1 mg/mL
technique(s)
ELISA: suitable, immunoblotting: suitable, immunofluorescence: suitable, immunohistochemistry: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... GALNT10(55568)
Immunogen
Antibody was raised against a 16 amino acid synthetic peptide near the amino terminus of human GALNT10.
Features and Benefits
Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.
Physical form
Supplied at 1 mg/mL in PBS with 0.02% sodim azide.
Other Notes
The action of this antibody can be blocked using blocking peptide SBP3500988.
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
12 - Non Combustible Liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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P Austin Nelson et al.
Brain research. Gene expression patterns, 1(2), 95-99 (2004-03-17)
Protein glycosylation is a common and important process that can alter the stability, half-life, biological activity and receptor recognition of target molecules. We have identified a new putative mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family member, termed GalNAc-T10/ppGaNTase-T10 (gene symbol Galnt10), and determined
M Amado et al.
Biochimica et biophysica acta, 1473(1), 35-53 (1999-12-02)
Enzymatic glycosylation of proteins and lipids is an abundant and important biological process. A great diversity of oligosaccharide structures and types of glycoconjugates is found in nature, and these are synthesized by a large number of glycosyltransferases. Glycosyltransferases have high
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