HPA008963
Anti-GALNT5 antibody produced in rabbit
Ab1, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-GalNAc-T5
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100 μL
$598.00
$598.00
Usually ships in 1 week. (Orders outside of US and Europe, please allow an additional 1-2 weeks for delivery)
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100 μL
$598.00
About This Item
$598.00
Usually ships in 1 week. (Orders outside of US and Europe, please allow an additional 1-2 weeks for delivery)
biological source
rabbit
Quality Level
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)
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:50-1:200
immunogen sequence
AERDLNVTISLSTDRPKQRSQAVANERAHPASTAVPKSGEAMALNKTKTQSKEVNANKHKANTSLPFPKFTVNSNRLRKQSINETPLGSLSKDDGARGAHGKKLNFSESHLVIITKEEEQKADPKEVSNSKTKTIFPKVLGKS
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... GALNT5(11227)
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General description
GALNT5 (N-acetylgalactosaminyltransferase 5) is a highly tissue specific protein. It predominantly localizes to the cytoplasm of gastric epithelial and gastric cancer cells. This gene localizes to human chromosome 2q24.[1]
Immunogen
polypeptide N-acetylgalactosaminyltransferase 5
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.
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
GALNT5 (N-acetylgalactosaminyltransferase 5) glycosylates restricted types of substrates. It is capable of interacting with Golgi proteins, by projecting its catalytic domain in the lumen of the Golgi complex. It might play a role in maintaining the structure of gastric mucosa, and less differentiated gastric tumor tissues show low expression of this protein. Its low expression is linked with TNM classification, and functions as an independent prognostic marker for poor outcome in gastric cancer patients.[1] In breast cancer, missense mutation in this gene results in the loss of enzymatic function of this GALNT5 protein. This gene is also up-regulated in hepatoblastomas when compared to the expression in differentiated livers.
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.
Linkage
Corresponding Antigen APREST71964
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
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Jiayi Yan et al.
American journal of cancer research, 13(10), 4579-4596 (2023-11-16)
Mucin-type O-glycosylation, a posttranslational modification of membrane and secretory proteins, facilitates metastasis and immune escape in tumor cells. N-acetylgalactosaminyl-transferase 5 (GALNT5), the enzyme initiating mucin-type O-glycosylation, is known to advance the progression of various tumors. Yet, the comprehensive role of
Muhammad Ramzan Manwar Hussain et al.
Journal of cellular biochemistry, 115(2), 313-327 (2013-09-17)
Aberrant glycosylation by N-acetylgalactosaminyl transferases (GALNTs) is a well-described pathological alteration that is widespread in hereditary diseases, prominently including human cancers, familial tumoral calcinosis and hyperostosis-hyperphosphatemia. In this study, we integrated different computational tools to perform the in silico analysis
Marutpong Detarya et al.
American journal of cancer research, 12(9), 4140-4159 (2022-10-14)
Cholangiocarcinoma (CCA) is a lethal cancer in that the incidence is now increasing worldwide. N-acetylgalactosaminyltransferase 5 (GALNT5), an enzyme that initiates the first step of mucin type-O glycosylation, has been reported to promote aggressiveness of CCA cells via the epithelial
Tatiane Cristina Rodrigues et al.
Future oncology (London, England), 10(15), 2449-2457 (2014-12-20)
Cytogenetic data of hepatoblastomas, a rare embryonal tumor of the liver, mostly consist of descriptions of whole-chromosome aneuploidies and large chromosome alterations. High-resolution cytogenetics may provide clues to hepatoblastoma tumorigenesis and indicate markers with clinical significance. We used array-CGH (180K)
H He et al.
British journal of cancer, 110(8), 2021-2029 (2014-03-13)
The family of polypeptide N-acetylgalactosaminyl transferases is responsible for the altered O-linked glycosylation occurring during the development of various cancers and their progression via altering O-glycan biosynthesis. Our studies were designed to investigate the expression and prognostic values of GalNAc-T5
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