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Merck

SAB4200400

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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A propos de cet article

NACRES:
NA.41
UNSPSC Code:
12352203

Principaux documents

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Nom du produit

Anti-WIPI-2 (C-terminal) antibody produced in rabbit, ~1.0 mg/mL, affinity isolated antibody

concentration

~1.0 mg/mL

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~49 kDa

species reactivity

mouse, rat, human

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.

UniProt accession no.

Q9Y4P8

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

Application

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

Biochem/physiol Actions

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.

Disclaimer

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.

General description

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.

Immunogen

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

Physical form

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

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Classe de stockage

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificats d'analyse (COA)

Lot/Batch Number
0000193769
0000183789
0000183789
0000193769
111M4780

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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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