biological source
rabbit
conjugate
unconjugated
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
technique(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunogen sequence
KVAGMSPWAPQVPVSPTPPYQRGHLPTGGHLAVCHFPCLLQEAQFHLQTQVFLQVR
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... GALNT14(79623)
General description
GALNT14 (polypeptide N-acetylgalactosaminyltransferase 14) belongs to UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family of proteins. It forms a subfamily with pp-GalNAc-T2, and contains the conserved motifs characteristic of pp-GalNAc-T family. It is a type II membrane protein, and is ubiquitously expressed, though it has the highest expression in kidney. This gene is located on human chromosome 2p23.1.
Immunogen
Polypeptide N-acetylgalactosaminyltransferase 14 recombinant protein epitope signature tag (PrEST)
Application
Anti-GALNT14 antibody is suitable for immunoprecipitation. Anti-GALNT14 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem/physiol Actions
GALNT14 (polypeptide N-acetylgalactosaminyltransferase 14) belongs to the family of proteins, which is involved in the first step of O-glycosylation of proteins in mammals. They achieve this by the transfer of N-acetyl-D-galactosamine (GalNAc) to their peptide substrates. As GALNT14 has the highest expression in kidney, GALNT14 might play a role in O-glycosylation in kidney. Studies show this protein regulates insulin-like growth factor binding protein-3 (IGFBP-3) mediated apoptosis, as well as insulin-like growth factor binding protein-3 (IGFBP-3)-mediated signaling pathway. It is up-regulated in a variety of cancers such as, breast, ovarian, lung and skin cancer. In pancreatic carcinoma, non-small-cell lung carcinoma and melanoma cell lines the expression of GALNT14 is correlated with the sensitivity to Apo2L/TRAIL pathway. It can be used as a marker in breast cancer to determine the histological grade. SNP rs9679162, in gene GALNT14 is useful in predicting the outcome of chemotherapy in patients with advanced hepatocellular carcinoma.
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:
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.
Physical form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Other Notes
Corresponding Antigen APREST72087.
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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存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
Ranran Wang et al.
Oncology reports, 30(2), 667-676 (2013-05-28)
A high expression of O-glycosylated proteins is one of the prominent characteristics of ovarian carcinoma cells associated with cell migration, which would be attributed to the upregulated expression of glycosyltransferases. Therefore, elucidating glycosyltransferases and their substrates may improve our understanding
Chau-Ting Yeh et al.
International journal of cancer, 134(5), 1214-1224 (2013-08-21)
Previously, a pilot genome-wide association study has identified candidate single nucleotide polymorphism predictors for the therapeutic response of 5-fluorouracil, mitoxantrone and cisplatin (FMP) combination chemotherapy in advanced hepatocellular carcinoma (HCC). Here, we conducted a prospective confirmatory study to examine the
Chen Wu et al.
Journal of biosciences, 34(3), 389-395 (2009-10-07)
Insulin-like growth factor binding protein-3 (IGFBP-3) is known to induce apoptosis in an insulin-like growth factor (IGF)-dependent and IGF-independent manner, but the mechanism underlying the IGF-independent effects remains unclear. Polypeptide N-acetylgalactosaminyltransferase 14 (GalNAc-T14) is a novel IGFBP-3 binding partner. In
Han Wang et al.
Biochemical and biophysical research communications, 300(3), 738-744 (2003-01-01)
A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) gene family was cloned and designated pp-GalNAc-T14. This type II membrane protein contains all motifs that are conserved in the pp-GalNAc-T family proteins and forms a subfamily with pp-GalNAc-T2 on the
Chen Wu et al.
BMC cancer, 10, 123-123 (2010-04-02)
The post-translational modification of proteins, including glycosylation, differs between normal and tumor cells. The UDP-N-acetyl-D-galactosamine polypeptide N-acetylgalactosaminyltransferases (GalNAc-Tases) family of enzymes regulates the initial steps of mucin O-glycosylation and is responsible for the altered glycosylation state observed in cancer cells.
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