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anti-Human PDCD6IP Antikörper:
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Human Polyclonal PDCD6IP Primary Antibody für WB - ABIN1881644
Inuzuka, Suzuki, Kawasaki, Shibata, Wakatsuki, Maki: Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in target recognition. in BMC structural biology 2010
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Human Monoclonal PDCD6IP Primary Antibody für IF, IHC (p) - ABIN2477348
Bechmann, Weiss: Regulation of the proton/electron stoichiometry of mitochondrial ubiquinol:cytochrome c reductase by the membrane potential. in European journal of biochemistry / FEBS 1991
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Human Polyclonal PDCD6IP Primary Antibody für IF, IHC - ABIN347079
Mahul-Mellier, Hemming, Blot, Fraboulet, Sadoul: Alix, making a link between apoptosis-linked gene-2, the endosomal sorting complexes required for transport, and neuronal death in vivo. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2006
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Human Polyclonal PDCD6IP Primary Antibody für IF, WB - ABIN6674282
Bei, Xu, Lv, Yu, Xu, Che, Das, Tigges, Toxavidis, Ghiran, Shah, Li, Zhang, Das, Xiao: Exercise-induced circulating extracellular vesicles protect against cardiac ischemia-reperfusion injury. in Basic research in cardiology 2018
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Mouse (Murine) Polyclonal PDCD6IP Primary Antibody für IF, WB - ABIN5664007
Zhao, Wu, Duan, Ma, Shen, Wei, Cui, Zhang, Xie, Liu: Quantitative proteomic analysis of exosome protein content changes induced by hepatitis B virus in Huh-7 cells using SILAC labeling and LC-MS/MS. in Journal of proteome research 2015
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Human Monoclonal PDCD6IP Primary Antibody für ICC, IF - ABIN260230
Haga, Yan, Takahashi, Matsuda, Patel: Extracellular Vesicles from Bone Marrow-Derived Mesenchymal Stem Cells Improve Survival from Lethal Hepatic Failure in Mice. in Stem cells translational medicine 2017
Human Polyclonal PDCD6IP Primary Antibody für IF, WB - ABIN523392
Kowal, Arras, Colombo, Jouve, Morath, Primdal-Bengtson, Dingli, Loew, Tkach, Théry: Proteomic comparison defines novel markers to characterize heterogeneous populations of extracellular vesicle subtypes. in Proceedings of the National Academy of Sciences of the United States of America 2016
our results identify the CD63-syntenin-1-ALIX complex as a key regulatory component in post-endocytic HPV trafficking.
Alix acts in concert with endophilin A to promote clathrin-independent endocytosis of cholera toxin and to regulate cell migration.
Revealed the transition of diffuse ALIX protein signals into a multivesicular body-like pattern during adenoma-carcinoma sequence in colorectal neoplasms.
Alix plays an important role in the proliferation of glioma cells and overexpression in gliomas predicts poor survival.
ALIX regulates P2Y1 degradation.
farnesylation of K-Ras was required for its packaging within extracellular nanovesicles, yet expressing a K-Ras farnesylation mutant did not decrease the number of nanovesicles or the amount of Alix protein released per cell.
These findings indicate that Alix binds to Ago2 and miRNAs, suggesting that it plays a key role in miRNA enrichment during extracellular vesicles biogenesis.
The authors find that HIV-1 nucleocapsid mimics the PDZ domains of syntenin, a membrane-binding adaptor involved in cell-to-cell contact/communication, to capture the Bro1 domain of ALIX, which is an ESCRTs recruiting cellular adaptor.
We found that ARRDC3 is required for ALIX ubiquitination induced by activation of PAR1
phosphorylation of the intramolecular interaction site in the PRD is one of the major mechanisms that activates the ESCRT function of ALIX
homologous domain of human Bro1 domain-containing proteins, Alix and Brox, binds CHMP4B but not STAM2, despite their high structural similarity
Accordingly, ALIX depletion leads to furrow regression in cells with chromosome bridges, a phenotype associated with abscission checkpoint signaling failure.
Findings indicate that the PDCD6IP 15bp insertion/deletion polymorphism decreases the risk of breast neoplasm in an Iranian population.
The serum lever of Alzheimer's disease were decrease and the expression of ALIX strongly correlated with the Mini-Mental State Examination scores of the AD patients
our findings identify heparanase as a modulator of the syndecan-syntenin-ALIX pathway, fostering endosomal membrane budding and the biogenesis of exosomes by trimming the heparan sulfate chains on syndecans
Our data reveal that AIP1, by inhibiting VEGFR2-dependent signaling in tumor niche, suppresses tumor EMT switch, tumor angiogenesis, and tumor premetastatic niche formation to limit tumor growth and metastasis.
Lack of ALG-2, ALIX or Vps4B each prevents shedding, and repair of the injured cell membrane
Alix is critically involved in multivesicular body sorting of membrane receptors in mammalian cells.
Aip1 has a role in actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring
ALIX is recruited to the neck of the assembling HIV-1 virion and is mostly recycled after virion release.
Alix-dependent, clathrin independent endocytosis is essential for controlling brain size.
By interacting with F-actin, the Par complex and ZO-1, Alix ensures the formation and maintenance of the apically restricted actomyosin-tight junction complex.
ATG12-ATG3 interacts with Alix to promote basal autophagic flux and late endosome function.
We have provided evidence that a promigratory function of galectin-3 may be mediated through interaction with its binding partner Alix.
Identify key role for syndecan-syntenin-ALIX in membrane transport and signalling processes.
the Ozz-E3 ligase regulates Alix at sites where the actin cytoskeleton undergoes remodeling.
Alix is a crucial mediator of Ca(2+) induced caspase 9 activation.
Biochemical characterization of two analogues of the apoptosis-linked gene 2 protein in Dictyostelium discoideum and interaction with murine Alix.
overexpression of Alix-CT leads to cytoplasmic vacuolization into tubulo-vesicular structures
interaction of Gag with Tsg101 and Alix favors budding from the plasma membrane and relieves a requirement for ubiquitination by Nedd4
tTe interaction of the ALG-2/Alix complex with TSG101 & CHMP4b is necessary for naturally occurring death of motoneurons. Alix represents a molecular link between the endolysosomal system and the cell death machinery.
These results eliminate the possibility that the two transcript variants encode different isoforms of Alix protein and suggest that alternative polyadenylation is one of the mechanisms controlling Alix protein expression.
a sub-population of Alix localizes extracellularly and regulates integrin-mediated cell adhesions and fibronectin matrix assembly.
E. faecalis strain-specific induction of colitis in IL-10-/- mice after 14 weeks of monoassociation. Our study suggests that Alix/AIP1 protein expression and ERK1/2 activation are decreased in severe colitis.
Data show that galectin-3 is an inhibitory regulator of T-cell activation and functions intracellularly by promoting TCR down-regulation, possibly through modulating Alix's function at the IS.
We conclude that ALIX and ESCRT-III coordinately control abscission in Drosophila fGSCs and that their complex formation is required for accurate abscission timing in GSCs in vivo.
These findings establish that Xp95/Alix is phosphorylated within the proline-rich domain during M-phase induction, and indicate that the phosphorylation may both positively and negatively modulate their interaction with partner proteins.
This gene encodes a protein that functions within the ESCRT pathway in the abscission stage of cytokinesis, in intralumenal endosomal vesicle formation, and in enveloped virus budding. Studies using mouse cells have shown that overexpression of this protein can block apoptosis. In addition, the product of this gene binds to the product of the PDCD6 gene, a protein required for apoptosis, in a calcium-dependent manner. This gene product also binds to endophilins, proteins that regulate membrane shape during endocytosis. Overexpression of this gene product and endophilins results in cytoplasmic vacuolization, which may be partly responsible for the protection against cell death. Several alternatively spliced transcript variants encoding different isoforms have been found for this gene. Related pseudogenes have been identified on chromosome 15.
ALG-2 interacting protein 1
, ALG-2-interacting protein X
, PDCD6-interacting protein
, apoptosis-linked gene 2-interacting protein X
, dopamine receptor interacting protein 4
, programmed cell death 6-interacting protein
, ALG-2-interacting protein 1
, Alg2-interacting protein 1
, Alg2-interacting protein X
, E2f1-inducible protein
, ALG-2 interacting protein X
, programmed cell death 6 interacting protein
, Programmed cell death 6 interacting protein
, putative signal tranduction protein Xp95
, signal transduction protein Xp95