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Merck

W2394

Sigma-Aldrich

Anti-WIPI-1 (C-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonim(y):

Anti-ATG18, Anti-WD repeat domain phosphoinositide interacting 1, Anti-WD40 repeat protein Interacting with phosphoInositides of 49kDa, Anti-WIPI-1 alpha, Anti-WIPI49

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About This Item

Kod UNSPSC:
12352203
NACRES:
NA.41

pochodzenie biologiczne

rabbit

białko sprzężone

unconjugated

forma przeciwciała

affinity isolated antibody

rodzaj przeciwciała

primary antibodies

klon

polyclonal

Postać

buffered aqueous solution

masa cząsteczkowa

antigen ~49 kDa

reaktywność gatunkowa

human, rat, mouse

stężenie

~1.0 mg/mL

metody

immunoprecipitation (IP): 5-10 μg using lysates of mouse 3T3 or at NRK cells
western blot: 2.5-5.0 μg/mL using whole extract of G-361 cells

numer dostępu UniProt

Warunki transportu

dry ice

temp. przechowywania

−20°C

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

human ... WIPI1(55062)
mouse ... Wipi1(52639)
rat ... Wipi1(303630)

Opis ogólny

WIPI-1, the mammalian orthologue of Atg18 in S. cerevisiae and A. thaliana, is a member of the WIPI subfamily of WD-repeat proteins. It has a 7-bladed propeller structure and contains a conserved motif for interaction with phospholipids. WIPI-1 is ubiquitously expressed in normal human tissues with highest levels in skeletal muscle, heart and testis. It is aberrantly expressed in human cancer.

Immunogen

synthetic peptide corresponding to amino acids 406-421 of human WIPI-1, conjugated to KLH. The corresponding sequence is identical in mouse and rat.

Zastosowanie

Anti-WIPI-1 (C-terminal) antibody produced in rabbit has been used in immunoblotting and immunoprecipitation.

Działania biochem./fizjol.

WIPI-1 has essential biological functions including signal transduction, transcription regulation and apoptosis. WD-repeat proteins regulate the assembly of multiprotein complexes by presenting a β-propeller platform for simultaneous and reversible protein-protein interactions. WIPI-1 is linked to starvation-induced autophagy.

Postać fizyczna

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.

Oświadczenie o zrzeczeniu się odpowiedzialności

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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Kod klasy składowania

10 - Combustible liquids

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

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


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Autophagosome formation in mammalian cells
Mizushima N, et al.
Cell Structure and Function, 27(6), 421-429 (2002)
WIPI-1alpha(WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy
Proikas-Cezanne T, et al.
Oncogene, 23(58), 9314-9314 (2004)
Maria Giovanna De Leo et al.
Autophagy, 17(11), 3644-3670 (2021-03-10)
Autophagosome formation requires PROPPIN/WIPI proteins and monophosphorylated phosphoinositides, such as phosphatidylinositol-3-phosphate (PtdIns3P) or PtdIns5P. This process occurs in association with mammalian endosomes, where the PROPPIN WIPI1 has additional, undefined roles in vesicular traffic. To explore whether these functions are interconnected
Thibault Courtellemont et al.
The EMBO journal, 41(10), e109646-e109646 (2022-04-26)
Endo-lysosomal compartments exchange proteins by fusing, fissioning, and through endosomal transport carriers. Thereby, they sort many plasma membrane receptors and transporters and control cellular signaling and metabolism. How the membrane fission events are catalyzed is poorly understood. Here, we identify

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