HPA011222
Anti-GALNT2 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
동의어(들):
Anti-GalNAc-T2, Anti-Polypeptide GalNAc transferase 2, Anti-Polypeptide N-acetylgalactosaminyltransferase 2, Anti-Protein-UDP acetylgalactosaminyltransferase 2, Anti-UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, Anti-pp-GaNTase 2
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모든 사진(4)
About This Item
추천 제품
생물학적 소스
rabbit
Quality Level
결합
unconjugated
항체 형태
affinity isolated antibody
항체 생산 유형
primary antibodies
클론
polyclonal
제품 라인
Prestige Antibodies® Powered by Atlas Antibodies
양식
buffered aqueous glycerol solution
종 반응성
human
기술
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:50-1:200
면역원 서열
SCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPALSQQWKFTLNL
UniProt 수납 번호
배송 상태
wet ice
저장 온도
−20°C
타겟 번역 후 변형
unmodified
유전자 정보
human ... GALNT2(2590)
일반 설명
GALNT2 (polypeptide N-acetylgalactosaminyltransferase 2) belongs to the ppGalNAc-T family, and is a type II transmembrane protein. The catalytic domain resides in the Golgi luminal region, and the R-type lectin domain lies in the C-terminal. This gene is localized to human chromosome 1q41-q42.
면역원
polypeptide N-acetylgalactosaminyltransferase 2
애플리케이션
Anti-GALNT2 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.
생화학적/생리학적 작용
GALNT2 (polypeptide N-acetylgalactosaminyltransferase 2) catalyzes the first step of O-linked glycosylation of proteins. It is responsible for the attachment of first N-acetylgalactosamine (GalNAc) monosaccharide to the protein. The expression of this gene is up-regulated in cancers, and it might be involved in tumorigenesis. It suppresses the expression of matrix metalloproteinase (MMP)-2 and transforming growth factor (TGF)-β1, and thus prevents proliferation and metastasis of gastric cancer cells. It modulates the development of placenta by regulating extravillus trophoblast (EVT) invasion. GALNT2 is also involved in insulin homeostasis by regulating the expression of ENPP1 (ectonucleotide pyrophosphatase), which is an inhibitor of insulin receptor signaling. Its expression is reduced in type 2 diabetes patients, and thus, it might play a role in hyperglycemia. It is up-regulated in oral squamous cell carcinoma (OSCC), and enhances the invasiveness of OSCC by modulating the O-glycosylation and activity of EGFR (epidermal growth factor receptor).
특징 및 장점
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.
결합
Corresponding Antigen APREST72034
물리적 형태
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
법적 정보
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
면책조항
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
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
가장 최신 버전 중 하나를 선택하세요:
Mei-Chun Lin et al.
Oral oncology, 50(5), 478-484 (2014-03-04)
Oral squamous cell carcinoma (OSCC) is one of the leading cancers worldwide. Aberrant glycosylation affects many cellular properties in cancers, including OSCC. This study aimed to explore the role of N-acetylgalactosaminyltransferase 2 (GALNT2) in OSCC. Immunohistochemistry was performed to study
Antonella Marucci et al.
PloS one, 8(7), e70159-e70159 (2013-07-31)
Impaired insulin action plays a major role in the pathogenesis of type 2 diabetes, a chronic metabolic disorder which imposes a tremendous burden to morbidity and mortality worldwide. Unraveling the molecular mechanisms underlying insulin resistance would improve setting up preventive
Wan-Ling Ho et al.
Oncotarget, 5(23), 12247-12259 (2014-11-05)
Aberrant expression of the simple mucin-type carbohydrate antigens such as Tn antigen is associated with malignant transformation and cancer progression. N-acetylgalactosaminyltransferase 2 (GALNT2), one of the enzymes that mediate the initial step of mucin-type O-glycosylation, is responsible for forming Tn
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
Romina B Cejas et al.
The Journal of biological chemistry, 294(9), 2997-3011 (2018-12-29)
Biological functions of nuclear proteins are regulated by post-translational modifications (PTMs) that modulate gene expression and cellular physiology. However, the role of O-linked glycosylation (O-GalNAc) as a PTM of nuclear proteins in the human cell has not been previously reported.
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