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ATP13A2 encodes a member of the P5 subfamily of ATPases which transports inorganic cations as well as other substrates. Additionally we are shipping ATP13A2 Proteins (9) and ATP13A2 Kits (3) and many more products for this protein.
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Human Polyclonal ATP13A2 Primary Antibody for EIA, WB - ABIN950560
Dos Santos, Pestana, Diniz, Campos, Abdalla-Carvalho, de Rosso, Pereira, Nicaretta, de Carvalho, Dos Santos, Santos-Rebouças, Pimentel: Mutational analysis of GIGYF2, ATP13A2 and GBA genes in Brazilian patients with early-onset Parkinson's disease. in Neuroscience letters 2010
Show all 5 references for ABIN950560
Human Monoclonal ATP13A2 Primary Antibody for ELISA, WB - ABIN393340
Reetz, Tadic, Kasten, Brüggemann, Schmidt, Hagenah, Pramstaller, Ramirez, Behrens, Siebner, Klein, Binkofski: Structural imaging in the presymptomatic stage of genetically determined parkinsonism. in Neurobiology of disease 2010
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Thsi stduy Our findings bring new insight into the biology of ATP13A2 and open novel opportunities for its study using zebrafish as a model organism.
tre (show TREH Antibodies) results of this study suggests that the expression of ATP13A2 regulated by the PHD2 (show EGLN1 Antibodies)-HIF1alpha (show HIF1A Antibodies) signaling pathway,and this is instrumental in maintaining cellular iron homeostasis and cell viability in mitochondrially compromised DAergic neurons.
that ATP13A2 contains a unique N-terminal hydrophobic extension that lies on the cytosolic membrane surface of the lysosome, where it interacts with the lysosomal signaling lipids phosphatidic acid and phosphatidylinositol(3,5)bisphosphate.
ATP13A2 overexpression improves the lysosome membrane integrity and protects against iron-induced cell damage.
A review of recent advances in the emerging association of ATP13A2 mutations with Parkinsonism and neuronal ceroid lipofuscinoses.
The mutation rates of Thr12Met and Ala1144Thr of ATP13A2 in the Uygur and Han Parkinson's disease patients in the Xinjiang region are low.
This study demonistrated that loss of ATP13A2 causes a specific protein trafficking defect, and that Atp13a2 null mice develop age-related motor dysfunction that is preceded by neuropathological changes.
Data show that patients with Lewy body diseases have an overall deficit in ATP13A2 protein levels, with the remaining protein being more insoluble and partially redistributing towards Lewy bodies
Present results of homozygosity mapping in two siblings affected with early onset Parkinson's disease (EOPD) and mutation screening of ATP13A2. The variation identified represents the 13th known disease causing mutation in ATP13A2.
these data suggest the involvement of PARK9 in the biogenesis of exosomes and alpha-synuclein (show SNCA Antibodies) secretion.
Reduced ATP13A2 expression significantly decreased vesicular zinc levels, indicating ATP13A2 facilitates transport of zinc.
the loss of Atp13a2 causes sensorimotor impairments, alpha-synuclein (show SNCA Antibodies) accumulation as occurs in PD and related synucleinopathies, and accumulation of lipofuscin deposits characteristic of NCL (show NCL Antibodies)
study reveals a number of intriguing neuronal phenotypes due to the loss- or gain-of-function of ATP13A2 that support a role for this protein in regulating intracellular cation homeostasis and neuronal integrity
This study showed that ATP13A2 regulates mitochondrial bioenergetics through macroautophagy.
This gene encodes a member of the P5 subfamily of ATPases which transports inorganic cations as well as other substrates. Mutations in this gene are associated with Kufor-Rakeb syndrome (KRS), also referred to as Parkinson disease 9. Multiple transcript variants encoding different isoforms have been found for this gene.
probable cation-transporting ATPase 13A2
, ATPase type 13A2
, probable cation-transporting ATPase 13A2-like
, putative ATPase