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Merck

SAB2102717

Sigma-Aldrich

Anti-WWP1 antibody produced in rabbit

affinity isolated antibody

Synonym(e):

Anti-AIP5, Anti-DKFZp434D2111, Anti-HSDRP1, Anti-Tiul1, Anti-WW domain containing E3 ubiquitin protein ligase 1

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100 μL
€ 423,00

€ 423,00


Versand innerhalb von 5 Werktagen. (Bei Bestellungen außerhalb der USA rechnen Sie bitte zusätzlich 1-2 Wochen für die Lieferung ein)


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100 μL
€ 423,00

About This Item

UNSPSC-Code:
12352203
NACRES:
NA.41

€ 423,00


Versand innerhalb von 5 Werktagen. (Bei Bestellungen außerhalb der USA rechnen Sie bitte zusätzlich 1-2 Wochen für die Lieferung ein)

Biologische Quelle

rabbit

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

105 kDa

Speziesreaktivität

dog, bovine, rat, rabbit, human

Konzentration

0.5 mg - 1 mg/mL

Methode(n)

immunohistochemistry: suitable
western blot: suitable

UniProt-Hinterlegungsnummer

Versandbedingung

wet ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... WWP1(11059)

Immunogen

Synthetic peptide directed towards the N terminal region of human WWP1

Biochem./physiol. Wirkung

WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. WWP1 is a protein which contains 4 tandem WW domains and a HECT (homologous to the E6-associated protein carboxyl terminus) domain. WWP1 belongs to a family of NEDD4-like proteins, which are E3 ubiquitin-ligase molecules and regulate key trafficking decisions, including targeting of proteins to proteosomes or lysosomes.WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. This gene encodes a protein which contains 4 tandem WW domains and a HECT (homologous to the E6-associated protein carboxyl terminus) domain. The encoded protein belongs to a family of NEDD4-like proteins, which are E3 ubiquitin-ligase molecules and regulate key trafficking decisions, including targeting of proteins to proteosomes or lysosomes. Alternative splicing of this gene generates at least 6 transcript variants; however, the full length nature of these transcripts has not been defined. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Sequenz

Synthetic peptide located within the following region: ATASPRSDTSNNHSGRLQLQVTVSSAKLKRKKNWFGTAIYTEVVVDGEIT

Physikalische Form

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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Die Dokumentenbibliothek aufrufen

Yongjian Li et al.
Cell death discovery, 8(1), 107-107 (2022-03-11)
WW domain-containing E3 ubiquitin protein ligase1 (WWP1) is reported to be upregulated in many types of human cancers; however, its expression and function in intrahepatic cholangiocarcinoma (ICC) remain unknown. Here, in this study we investigated the expression pattern, clinical prognosis
Jianwei Li et al.
Nature communications, 10(1), 1589-1589 (2019-04-10)
Transmembrane and coiled-coil domains 1 (TMCO1) is a recently identified Ca2+ leak channel in the endoplasmic reticulum. TMCO1 dysfunction in humans is associated with dysmorphism, mental retardation, glaucoma and the occurrence of cancer. Here we show an essential role of

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