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vps35 belongs to a group of vacuolar protein sorting (VPS) genes. Zusätzlich bieten wir Ihnen vps35 Proteine (3) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 45 products:
Chinese Hamster Polyclonal vps35 Primary Antibody für ICC, IF - ABIN250175
Hong, Yang, Zhang, Niu, Li, Zhao, Liu: The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport. in Cell research 2009
Show all 14 Pubmed References
Human Monoclonal vps35 Primary Antibody für ELISA, WB - ABIN565910
Prosser, Tran, Schooley, Wendland, Ngsee: A novel, retromer-independent role for sorting nexins 1 and 2 in RhoG-dependent membrane remodeling. in Traffic (Copenhagen, Denmark) 2010
Show all 3 Pubmed References
Human Polyclonal vps35 Primary Antibody für IHC, ELISA - ABIN185182
Zhang, Yu, Gao, Fu, Dai, Zhao, Zheng, Zhao: Cloning and characterization of human VPS35 and mouse Vps35 and mapping of VPS35 to human chromosome 16q13-q21. in Genomics 2001
Show all 2 Pubmed References
Human Polyclonal vps35 Primary Antibody für IHC, IHC (p) - ABIN4365839
Yin, Liu, He, Zhou, Yuan, Zhao: Vps35-dependent recycling of Trem2 regulates microglial function. in Traffic (Copenhagen, Denmark) 2016
The in vivo effects of P316S, D620N and L774M of VPS35 using Drosophila as a model, were investigated.
The findings of this study indicate that the VPS35 may play a crucial role in alpha-synucle in degradation by modulating the maturation of cathepsin D (zeige CTSD Antikörper) and might thereby contribute to the pathogenesis of the disease.
overexpression of Vps35 ameliorates the pathogenic mutant LRRK2 (zeige LRRK2 Antikörper) eye phenotype in a Drosophila model of Parkinson's disease
Vps35 negatively regulates actin (zeige ACTB Antikörper) polymerisation, and genetic interactions suggest that some of the endocytic and signalling defects of vps35 mutants are due to this function
Results provide evidence for a critical role of Vps35 in mouse corneal dystrophy; suggest that SLC4A11 (zeige SLC4A11 Antikörper) appears to be a Vps35/retromer cargo, and Vps35-regulation of SLC4A11 (zeige SLC4A11 Antikörper) trafficking may underlie Vps35/retromer regulation of corneal dystrophy.
Our study suggests that Vps35/retromer is responsible for recycling of Trem2 (zeige TREM2 Antikörper) in the regulation of microglial function such as proinflammatory responses.
Using in vivo knockdown of the critical retromer component VPS35, we demonstrate a specific role for this endosomal sorting complex in the trafficking of AMPA (zeige GRIA3 Antikörper) receptors during NMDA-receptor-dependent LTP (zeige SCP2 Antikörper) at mature hippocampal synapses.
the data presented in this manuscript demonstrate a critical function of VPS35 in regulating PTH1R (zeige PTH1R Antikörper) trafficking. This event and VPS35-interaction with PPP1R14C (zeige PPP1R14C Antikörper) appear to be essential for turning off PTH1R's endosomal signaling, and promoting PTH1R (zeige PTH1R Antikörper)-mediated catabolic response and bone remodeling.
These results provide evidence for VPS35's function in promoting spine maturation, which is likely through increasing AMPA (zeige GRIA3 Antikörper) receptor targeting to the postsynaptic membrane.
Deletion of the VPS35 gene in dopamine (DA) neurons resulted in Parkinson disease-like deficits, including loss of DA neurons and accumulation of alpha-synuclein.
These results suggest that VPS35 deficiency or mutation promotes Parkinson Disease (PD) pathogenesis, and reveals a crucial pathway, VPS35-Lamp2a-alpha-synuclein, to prevent PD pathogenesis.
Our studies reveal unexpected genetic and functional interactions between VPS35 and EIF4G1, two seemingly unrelated PD genes, and functionally connect them to alpha-synuclein pathobiology in yeast, worms, and mouse.
Vps35 is necessary for mouse retinal ganglion cell survival and regeneration.
VPS35 critically deregulates RANK signaling, thus restraining increased formation of hyperresorptive OCs and preventing osteoporotic deficits.
These findings provide new mechanistic insights into the role of VPS35 in the regulation of AIMP2 (zeige AIMP2 Antikörper) levels and cell death.
The retromer complex is a highly conserved membrane trafficking assembly composed of three proteins - Vps26 (zeige VPS26A Antikörper), Vps29 (zeige VPS29 Antikörper) and Vps35, which are impaired in neurodegenerative diseases. (Review)
It could interact with DRD1 (zeige DRD1 Antikörper) and regulate DRD1 (zeige DRD1 Antikörper) cell surface recycling, as well as DRD1 (zeige DRD1 Antikörper)- mediated dopamine signaling.
The absence of mutations in VPS35 genes reveals that they are uncommon causes of Parkinson disease in Brazil
VPS35 has been associated with autosomal dominant forms of Parkinson's disease with a high but incomplete penetrance .
results lend further support to the notion that VPS35-DLP1 (zeige DNM1L Antikörper) interaction is key to the retromer-dependent recycling of mitochondrial DLP1 (zeige DNM1L Antikörper) complex during mitochondrial fission and provide a novel therapeutic target to control excessive fission and associated mitochondrial deficits.
Silencing VPS35 increased N-Ras's association with cytoplasmic vesicles, diminished GTP (zeige AK3 Antikörper) loading of Ras, and inhibited mitogen-activated protein kinase (zeige MAPK1 Antikörper) signaling and growth of N-Ras (zeige NRAS Antikörper)-dependent melanoma cells.
deletion of VPS35 in yeast (vps35Delta) leads to a dose-dependent growth defect towards copper. This increased sensitivity could be rescued by transformation with yeast wild-type VPS35 but not by the expression of a construct harboring the yeast equivalent (i.e. D686N) of the most commonly identified VPS35-associated Parkinson disease mutation, p.D620N
the Vps35 R524W-containing retromer has a decreased endosomal association, which can be partially rescued by R55, a small molecule previously shown to stabilize the retromer complex, supporting the potential for future targeting of the retromer complex in the treatment of Parkinson disease.
X-ray crystallographic analysis of a 4-component complex comprising the VPS26 (zeige VPS26A Antikörper) & VPS35 subunits of retromer, sorting nexin SNX3 (zeige SNX3 Antikörper), & recycling signal from the divalent cation transporter DMT1 (zeige DMRT1 Antikörper)-II; analysis identifies a binding site for canonical recycling signals at the interface between VPS26 (zeige VPS26A Antikörper) & SNX3 (zeige SNX3 Antikörper); shows cooperative interactions among the VPS subunits, SNX3 (zeige SNX3 Antikörper) & cargo that couple signal-recognition to membrane recruitment.
This gene belongs to a group of vacuolar protein sorting (VPS) genes. The encoded protein is a component of a large multimeric complex, termed the retromer complex, involved in retrograde transport of proteins from endosomes to the trans-Golgi network. The close structural similarity between the yeast and human proteins that make up this complex suggests a similarity in function. Expression studies in yeast and mammalian cells indicate that this protein interacts directly with VPS35, which serves as the core of the retromer complex.
vacuolar protein sorting-associated protein 35
, vacuolar protein sorting 35 homolog (S. cerevisiae)
, vacuolar protein sorting 35 homolog
, vacuolar protein sorting 35-like
, vacuolar protein sorting 35
, Vacuolar protein sorting 35
, maternal embryonic message 3
, maternal-embryonic 3
, vesicle protein sorting 35