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Key Documents

SAB4200400

Sigma-Aldrich

Anti-WIPI-2 (C-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonyme(s) :

Anti-ATG18B, Anti-Atg21, Anti-CGI-50, Anti-WD repeat domain, phosphoinositide interacting 2, Anti-WIPI2

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~49 kDa

Espèces réactives

mouse, rat, human

Concentration

~1.0 mg/mL

Technique(s)

immunoprecipitation (IP): 2.5-5.0 μg using lysates of rat NRK cells.
western blot: 2-4 μg/mL using whole extracts of human G-361 and NIH-3T3 cells.

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... WIPI2(26100)
mouse ... Wipi2(74781)
rat ... Wipi2(288498)

Description générale

WIPI-2 belongs to the WIPI subfamily of WD40 repeat proteins. It is widely expressed in a variety of cell lines. The protein is characterized with a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids. It is a membrane constituent of autophagosomes and the plasma membrane.

Immunogène

synthetic peptide corresponding to the C-terminal region of human WIPI-2, conjugated to KLH. The corresponding sequence is identical in mouse and rat.

Application

Anti-WIPI-2 (C-terminal) antibody produced in rabbit may be used in various immunochemical techniques including
  • immunoblotting
  • immunoprecipitation
  • immunostaining.

Actions biochimiques/physiologiques

WIPI subfamily proteins acts as a key component of many essential biological functions such as signal transduction, transcription regulation and apoptosis. WIPI-2 is a phosphatidylinositol-3-phosphate binding protein that is needed for starvation induced autophagy. In addition, it is also essential for LC3 lipidation and it is linked to early autophagosomal structures together with Atg16L and ULK1.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Autophagosomal YKT6 is required for fusion with lysosomes independently of syntaxin 17
Matsui T, et al.
The Journal of cell biology, 217(8), 2633-2645 (2018)
Differential requirement for ATG2A domains for localization to autophagic membranes and lipid droplets
Tamura N, et al.
Febs Letters, 591(23), 3819-3830 (2017)
Kenta Imai et al.
Journal of cell science, 129(20), 3781-3791 (2016-09-03)
Autophagy is an intracellular degradation pathway conserved in eukaryotes. Among core autophagy-related (Atg) proteins, mammalian Atg9A is the sole multi-spanning transmembrane protein, and both of its N- and C-terminal domains are exposed to the cytoplasm. It is known that Atg9A
Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation.
Polson HE
Autophagy, 6(4), 506-522 (2010)
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)

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