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VPS29 belongs to a group of vacuolar protein sorting (VPS) genes that, when functionally impaired, disrupt the efficient delivery of vacuolar hydrolases. Zusätzlich bieten wir Ihnen Vacuolar Protein Sorting 29 Homolog (S. Cerevisiae) Proteine (19) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 51 products:
Human Polyclonal VPS29 Primary Antibody für ELISA, WB - ABIN250157
Haft, de la Luz Sierra, Bafford, Lesniak, Barr, Taylor: Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes. in Molecular biology of the cell 2000
Human Polyclonal VPS29 Primary Antibody für IHC (p), IHC - ABIN251587
Nakada-Tsukui, Saito-Nakano, Ali, Nozaki: A retromerlike complex is a novel Rab7 effector that is involved in the transport of the virulence factor cysteine protease in the enteric protozoan parasite Entamoeba histolytica. in Molecular biology of the cell 2005
Human Polyclonal VPS29 Primary Antibody für ELISA, WB - ABIN565652
Miura, Hasegawa, Konno, Suzuki, Sugeno, Fujikake, Geisler, Tabuchi, Oshima, Kikuchi, Baba, Wada, Nagai, Takeda, Aoki: VPS35 dysfunction impairs lysosomal degradation of ?-synuclein and exacerbates neurotoxicity in a Drosophila model of Parkinson's disease. in Neurobiology of disease 2014
Human Polyclonal VPS29 Primary Antibody für ICC, IF - ABIN4365830
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. in Nature methods 2013
The retromer complex is a highly conserved membrane trafficking assembly composed of three proteins - Vps26 (zeige VPS26A Antikörper), Vps29 and Vps35 (zeige vps35 Antikörper), which are impaired in neurodegenerative diseases. (Review)
Heterotrimer composed of DSCR3 (zeige DSCR3 Antikörper), C16orf62 and VPS29 orchestrates endosomal cargo retrieval and recycling.
This study demonstrated that Genetic variability of VPS29 in parkinsonism.
Data indicate that vesicular transport proteins VPS35 (zeige vps35 Antikörper) and VPS29 influence the levels of the other subunit of retromer.
Conclusion is that VPS29 is a metal ion-independent, rigid scaffolding domain, which is essential but not sufficient for incorporation of retromer into functional endosomal transport assemblies.
analysis of the phosphodiesterase/nuclease (zeige DCLRE1C Antikörper)-like fold and two protein-protein interaction sites in human VPS29
It was demonstrated that recombinant human Vps29 displays in vitro phosphatase activity towards a serine-phosphorylated peptide, containing the acidic-cluster dileucine motif of the cytoplasmatic tail of the CI-M6PR (zeige IGF2R Antikörper).
These observations indicate that the mammalian retromer complex assembles by sequential association of SNX1 (zeige SNX1 Antikörper)/2 and Vps26 (zeige VPS26A Antikörper)-Vps29-Vps35 (zeige vps35 Antikörper) subcomplexes on endosomal membranes and that SNX1 (zeige SNX1 Antikörper) and SNX2 (zeige SNX2 Antikörper) play interchangeable but essential roles.
crystal structure of a VPS29-VPS35 (zeige vps35 Antikörper) subcomplex showing how the metallophosphoesterase-fold subunit VPS29 acts as a scaffold for the carboxy-terminal half of VPS35 (zeige vps35 Antikörper)
Membrane recruitment of the cargo-selective retromer subcomplex VPS35 (zeige vps35 Antikörper)/29/26 is catalysed by the small GTPase (zeige RACGAP1 Antikörper) Rab7 (zeige RAB7B Antikörper) and inhibited by the Rab (zeige HRB Antikörper)-GAP TBC1D5 (zeige TBC1D5 Antikörper).
These results suggest that mouse Vps26b (zeige VPS26B Antikörper)-Vps29-Vps35 (zeige vps35 Antikörper) retromer complex is implicated in the transport of sortilin (zeige SORT1 Antikörper) from endosomes to the trans-Golgi network.
Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly.
VPS29 plays a crucial role in recycling VSRs from the PVC to the trans-Golgi network during the trafficking of soluble proteins to the lytic vacuole .
A combination of immunoelectron and fluorescence microscopy show that VPS29p localize to the trans-Golgi network (TGN (zeige TG Antikörper)), which is considered to represent the early endosome of plants.
Findings suggest that MAG1/VPS29 protein is involved in recycling a plant receptor for the efficient sorting of seed storage proteins
VPS29 is required for endosome homeostasis, PIN (zeige DYNLL1 Antikörper) protein cycling, and dynamic PIN1 repolarization during plant organ development.
This gene belongs to a group of vacuolar protein sorting (VPS) genes that, when functionally impaired, disrupt the efficient delivery of vacuolar hydrolases. The protein encoded by this gene is a component of a large multimeric complex, termed the retromer complex, which is involved in retrograde transport of proteins from endosomes to the trans-Golgi network. This VPS protein may be involved in the formation of the inner shell of the retromer coat for retrograde vesicles leaving the prevacuolar compartment. Alternative splice variants encoding different isoforms, and usage of multiple polyadenylation sites have been found for this gene.
, retromer protein
, vacuolar protein sorting-associated protein 29
, vacuolar sorting protein VPS29/PEP11
, vesicle protein sorting 29
, x 007 protein
, vacuolar sorting protein 29
, Vesicle protein sorting 29
, vacuolar protein sorting 29 homolog
, Vacuolar protein sorting-associated protein 29
, vacuolar protein sorting 29 homolog (S. cerevisiae)
, hypothetical protein
, protein involved in endosome to golgi protein transport
, subunit of retromer complex
, vacuolar protein sorting 29