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The protein encoded by PICK1 contains a PDZ domain, through which it interacts with protein kinase C, alpha (PRKCA). Additionally we are shipping PICK1 Kits (21) and PICK1 Proteins (10) and many more products for this protein.
Showing 10 out of 107 products:
Mouse (Murine) Polyclonal PICK1 Primary Antibody for ELISA, WB - ABIN185725
Steinberg, Takamiya, Shen, Xia, Rubio, Yu, Jin, Thomas, Linden, Huganir: Targeted in vivo mutations of the AMPA receptor subunit GluR2 and its interacting protein PICK1 eliminate cerebellar long-term depression. in Neuron 2006
Human Polyclonal PICK1 Primary Antibody for WB - ABIN391109
Xue, Zhang, Chen, Lin, Shi: PDZ protein mediated activity-dependent LTP/LTD developmental switch at rat retinocollicular synapses. in American journal of physiology. Cell physiology 2010
ICA1L forms BAR-domain complexes with PICK1 and is crucial for acrosome formation in spermiogenesis.
results indicate that PICK1 is a crucial regulator in glutathione homeostasis and may play important roles in oxidative stress.
In cultured neurons, PICK1 deletion increases surface AMPARs and blocks Abeta42-induced reduction in surface GluA2 (show GRIA2 Antibodies).
This study demonstrated that PICK1 functions in vesicle biogenesis and is necessary to maintain normal vesicle numbers and size.
C-terminal domain of ICA69 (show ICA1 Antibodies) interacts with PICK1 and acts on trafficking of PICK1-PKCalpha (show PKCa Antibodies) complex and cerebellar plasticity.
we found that PICK1's expression in testis rescued the spermatogenic abnormalities and male infertility in Pick1 knockout mice. Our results indicate that the infertility is caused by the lack of PICK1 in the testis rather than in other organs.
PICK1 is a critical DHHC8 (show ZDHHC8 Antibodies) substrate whose palmitoylation is necessary for long-term depression
PICK1 and ICA69 (show ICA1 Antibodies) are key regulators of the formation and maturation of insulin (show INS Antibodies) granules.
PICK1, together with ICA69 (show ICA1 Antibodies), is critical during budding of immature secretory vesicles from the trans-golgi network and thus for vesicular hormone storage.
PICK1 appears to be required for peripheral nerve injury-induced neuropathic pain development and to be a potential biochemical target for treating this disorder.
PICK1 domain ACT links PICK1-associated vesicles to a motility factor, likely myosin, but, contrary to previous reports, PICK1 neither binds nor inhibits Arp2 (show ACTR2 Antibodies)/3 complex.
Unlike accessory domains in other BAR domain proteins, the positioning of the PDZ domains is flexible, enabling PICK1 to perform long-range, dynamic scaffolding of membrane-associated proteins.
Data indicate three principal binding modes can account for protein interacting with C-kinase 1 (PICK1) PDZ domains binding specificity.
PICK1 promotes Ago2 (show EIF2C2 Antibodies) localization at endosomal compartments in neuronal dendrites and inhibits Ago2 (show EIF2C2 Antibodies) function in translational repression following neuronal stimulation.
These data indicate that Pick1 is involved in regulating the cell-cell junction in epithelial cells.
Family-based association study failed to observe a statistically significant association for any of the genotyped SNPs in the PICK1 gene and attention-deficit hyperactivity disorder.
PICK1 increases caveolin-mediated endocytosis, ubiquitination and degradation of TGF-beta type I receptor (show TGFBR1 Antibodies).
The binding affinities of all major PICK1 interacting proteins are reported and the effects of PICK1 mutations on these interactions are described.
Our data suggest a selective role of PICK1 in clustering and reducing the recycling rates of PDZ domain binding partners sorted to the Rab11-dependent recycling pathway.
The protein encoded by this gene contains a PDZ domain, through which it interacts with protein kinase C, alpha (PRKCA). This protein may function as an adaptor that binds to and organizes the subcellular localization of a variety of membrane proteins. It has been shown to interact with multiple glutamate receptor subtypes, monoamine plasma membrane transporters, as well as non-voltage gated sodium channels, and may target PRKCA to these membrane proteins and thus regulate their distribution and function. This protein has also been found to act as an anchoring protein that specifically targets PRKCA to mitochondria in a ligand-specific manner. Three transcript variants encoding the same protein have been found for this gene.
, protein kinase C, alpha binding protein
, protein kinase C-alpha-binding protein
, protein that interacts with C kinase 1
, protein interacting with C kinase 1