WD Repeat Domain, Phosphoinositide Interacting 2 Proteine (WIPI2)

WD40 repeat proteins are key components of many essential biologic functions. Zusätzlich bieten wir Ihnen WIPI2 Antikörper (81) und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
WIPI2 26100 Q9Y4P8
Maus WIPI2 WIPI2 74781 Q80W47
Ratte WIPI2 WIPI2 288498 Q6AY57
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Top WIPI2 Proteine auf antikoerper-online.de

Showing 4 out of 4 products:

Katalog Nr. Origin Quelle Konjugat Bilder Menge Anbieter Lieferzeit Preis Details
Insektenzellen Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 56 Days
7.380,00 €
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HOST_Wheat germ Human GST tag 10 μg Anmelden zum Anzeigen 7 bis 8 Tage
345,60 €
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Hefe Xenopus laevis His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
3.062,54 €
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Hefe Yeast His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
3.244,12 €
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WIPI2 Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human ,
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Weitere Proteine zu WD Repeat Domain, Phosphoinositide Interacting 2 (WIPI2) Interaktionspartnern

Human WD Repeat Domain, Phosphoinositide Interacting 2 (WIPI2) Interaktionspartner

  1. Here the authors show that recruitment of WIPI2, itself essential for anti-bacterial autophagy, is dependent on the localization of catalytically active TBK1 (zeige TBK1 Proteine) to the vicinity of cytosolic bacteria.

  2. The specific autophagosomal localization of both WIPI1 (zeige WIPI1 Proteine) and WIPI2 (refered to as WIPI puncta) has been employed to assess autophagy using fluorescence microscopy methods, such as confocal and live-cell video microscopy

  3. Data suggest WIPI1/WIPI2 (zeige WIPI1 Proteine) co-localize with microtubule-associated light chain 3 and autophagy related proteins 2/14L, participate in biogenesis of phagosomes, autophagy, and mobilization of lipids to/from intracellular droplets. [review-like article]

  4. WIPI-1 (zeige WIPI1 Proteine) and WIPI-2 are functionally required in mediating the PI3P signal at the onset of autophagy in NB4 cells.

  5. Data suggest that WIPI2b directly interacts with dimer of ATG16L1 (autophagy related 16-like 1 (zeige ATG16L1 Proteine)) and this interaction is linked to production of phosphatidylinositol 3-phosphate in endoplasmic reticulum triggered by autophagosome formation. [REVIEW]

  6. WIPI2b binds the membrane surrounding Salmonella and recruits the Atg12 (zeige ATG12 Proteine)-5-16L1 complex, initiating LC3 (zeige MAP1LC3A Proteine) conjugation, autophagosomal membrane formation, and engulfment of Salmonella.

  7. WIPI2 is a phosphatidylinsitol-3-phosphate binding protein required for starvation induced autophagy.

  8. Freeze-fracture replica immunolabelling reveals WD-repeat protein (zeige DCAF7 Proteine) interacting with phosphoinositides 1 and 2 (WIPI-1 (zeige WIPI1 Proteine) and WIPI-2) as membrane components of autophagosomes and the plasma membrane (PM).

WIPI2 Protein Überblick

Protein Überblick

WD40 repeat proteins are key components of many essential biologic functions. They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein-protein interactions. Members of the WIPI subfamily of WD40 repeat proteins, such as WIPI2, have a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids (Proikas-Cezanne et al., 2004

Genbezeichner und Symbole assoziert mit WIPI2

  • WD repeat domain phosphoinositide-interacting protein 2 (wipi2)
  • WD repeat domain, phosphoinositide interacting 2 (WIPI2)
  • WD repeat domain, phosphoinositide interacting 2 (Wipi2)
  • 1110018O08Rik Protein
  • 2510001I10Rik Protein
  • ATG18B Protein
  • Atg21 Protein
  • WIPI-2 Protein

Bezeichner auf Proteinebene für WIPI2

WIPI-2 , WD repeat domain phosphoinositide-interacting protein 2 , WD40 repeat protein interacting with phosphoinositides 2 , WIPI49-like protein 2

GENE ID SPEZIES
380011 Xenopus laevis
26100 Homo sapiens
74781 Mus musculus
288498 Rattus norvegicus
416481 Gallus gallus
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