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Merck

HPA023180

Sigma-Aldrich

Anti-WWP1 antibody produced in rabbit

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

别名:

Anti-AIP5, Anti-DKFZP434D2111, Anti-SCM-1b, Anti-SCYC2, Anti-WW domain containing E3 ubiquitin protein ligase 1

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About This Item

分類程式碼代碼:
12352203
人類蛋白質圖譜編號:
NACRES:
NA.41

生物源

rabbit

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

產品線

Prestige Antibodies® Powered by Atlas Antibodies

形狀

buffered aqueous glycerol solution

物種活性

human

技術

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

免疫原序列

TIDLKQALLIHNRKLERVKEQLKLSLENKNGIAQTGELTVVLDGLVIEQENITNCSSSPTIEIQENGDALHENGEPSARTTARLAVEGTNGIDNHV

UniProt登錄號

運輸包裝

wet ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... WWP1(11059)

一般說明

WWP1 (WW domain containing E3 ubiquitin protein ligase 1) is a member of the Nedd4 (neural precursor cell-expressed developmentally downregulated 4) family. The gene is mapped to human chromosome 8q21. The protein has a C2 calcium binding domain, four WW domains, and a HECT (homologous to the E6-AP carboxyl terminus) domain.

免疫原

WW domain containing E3 ubiquitin protein ligase 1 recombinant protein epitope signature tag (PrEST)

應用

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.

生化/生理作用

WWP1 (WW domain containing E3 ubiquitin protein ligase 1) is an E3 ubiquitin ligase. It is a putative target of microRNA (miR)-21, a miRNA which is upregulated in various cancers. In addition, it is upregulated in prostate, breast cancers and hepatocellular carcinoma (HCC). In HCC, it is linked with growth and cell survival. WWP1 suppresses TGF (transformiang growth factor)-β signaling by interacting with SMAD7 (Mothers against decapentaplegic homolog 7). It causes the degradation of TGFβ type I receptor. WWP1 is also involved in bone differentiation and metastasis, and EGF (epidermal growth factor) signaling.

特點和優勢

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.

聯結

Corresponding Antigen APREST76231

外觀

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide.

法律資訊

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

免責聲明

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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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Zhiyu Wang et al.
International journal of oncology, 45(4), 1469-1478 (2014-07-23)
Prostate cancer is the most common malignancy diagnosed in males, and bone metastases remain a significant source of morbidity and mortality in this population. Ubiquitin ligase E3s and proteasomes were thought to play essential roles in the development of cancers
Keqiang Zuo et al.
International journal of clinical and experimental pathology, 8(1), 414-422 (2015-03-11)
Endothelial damage is strongly associated with cardiovascular diseases such as atherosclerosis. Bone marrow-derived endothelial progenitor cells (EPCs) play an important role in the maintenance of endothelial homeostasis and contribute to re-endothelialization of injured vessels as well as revascularization of ischemic
Qian Cheng et al.
Biochemical and biophysical research communications, 448(3), 248-254 (2014-05-06)
The activation of oncogenes and the loss of tumor suppressor genes are believed to play critical roles in the pathogenesis of human hepatocellular carcinoma (HCC). The human WW domain containing E3 ubiquitin protein ligase 1 (WWP1) gene is frequently amplified
Benjamin Yeung et al.
PloS one, 8(4), e61027-e61027 (2013-04-11)
The Large Tumor Suppressor 1 (LATS1) is a serine/threonine kinase and tumor suppressor found down-regulated in various human cancers. LATS1 has recently been identified as a central player of the emerging Hippo signaling pathway, which plays important roles in organ
Thomas Courivaud et al.
The Journal of biological chemistry, 290(34), 21007-21018 (2015-07-15)
Although E3 ubiquitin ligases are deemed to play key roles in normal cell function and homeostasis, whether their alterations contribute to cancer pathogenesis remains unclear. In this study, we sought to investigate potential mechanisms that govern WWP1/Tiul1 (WWP1) ubiquitin ligase

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