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Merck

HPA011222

Sigma-Aldrich

Anti-GALNT2 antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

別名:

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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About This Item

UNSPSCコード:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

由来生物

rabbit

結合体

unconjugated

抗体製品の状態

affinity isolated antibody

抗体製品タイプ

primary antibodies

クローン

polyclonal

製品種目

Prestige Antibodies® Powered by Atlas Antibodies

形状

buffered aqueous glycerol solution

化学種の反応性

human

テクニック

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:50-1:200

免疫原配列

SCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPALSQQWKFTLNL

UniProtアクセッション番号

輸送温度

wet ice

保管温度

−20°C

ターゲットの翻訳後修飾

unmodified

遺伝子情報

human ... GALNT2(2590)

詳細

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.

免疫原

polypeptide N-acetylgalactosaminyltransferase 2

アプリケーション

Prestige抗体®は、Human Proteome Resource(HPR)プロジェクト(www.proteinatlas.org)によって開発・実証されたAtlas抗体です。抗体はすべて、数百の正常組織・疾病組織に対する免疫組織染色試験を行っています。これらの染色画像はHuman Protein Atlas(HPA)サイトで[Image Gallery]リンクをクリックするとご覧いただけます。さらに、ほとんどのPrestige抗体はプロテインアレイおよびウェスタンブロッティングの試験を行っています。試験のプロトコールおよびPrestige抗体、HPAに関する情報はsigma.com/prestigeをご覧ください。

生物化学的/生理学的作用

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).

特徴および利点

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.

関連事項

Corresponding Antigen APREST72034

物理的形状

PBS溶液(pH 7.2, 40%グリセロールおよび0.02%アジ化ナトリウム含有)。

法的情報

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

免責事項

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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保管分類コード

10 - Combustible liquids

WGK

WGK 1

引火点(°F)

Not applicable

引火点(℃)

Not applicable

個人用保護具 (PPE)

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

Jan Code

HPA011222-100UL:
HPA011222-25UL:


試験成績書(COA)

製品のロット番号・バッチ番号を入力して、試験成績書(COA) を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。

以前この製品を購入いただいたことがある場合

文書ライブラリで、最近購入した製品の文書を検索できます。

文書ライブラリにアクセスする

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.

ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.

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