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inositol 1,4,5-trisphosphate binding protein [RGD, Feb 2006].. Zusätzlich bieten wir Ihnen PLCL1 Antikörper (53) und PLCL1 Proteine (6) und viele weitere Produktgruppen zu diesem Protein an.
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susceptibility gene for dermatomyositis in Chinese patients with idiopathic inflammatory myopathies
PRIP interacts with the catalytic subunits of PP1 and PP2A and the interactions are regulated by phosphorylation. [review]
effect of DZP on PRIP-1 knockout mice was reduced
In postmenopausal women, our results suggest that the PLCL1 rs7595412 polymorphism has no obvious effect on hip bone size and bone mineral density but may be associated with increased proportion of vertebral fracture and increased levels of osteocalcin
PRIP-1 plays an important role in type A receptor signaling for gamma-aminobutyric acid in the brain
PLCL1 is a novel gene associated with variation in hip bone size, which has a role in the pathogenesis of hip fractures
Phospholipase C-related catalytically inactive protein (PRIP)-deficient mouse embryonic fibroblasts exhibited increased cell migration, and was significantly attenuated upon transfection with a siRNA targeting p110alpha, a catalytic subunit of class I phosphoinositide 3-kinases (PIK3CA).
These results suggest that PRIPs are positively involved in the development of follicles via their regulation of LH-LHR signaling and estradiol secretion.
Data show that PRIP is required for the fusion of Staphylococcus aureus-containing autophagosome-like vacuoles with lysosomes, indicating that PRIP is a novel modulator in the regulation of the innate immune system in non-phagocytic host cells.
PRIP promotes the translocation of phosphatases to lipid droplets to trigger the dephosphorylation of HSL and perilipin A, thus reducing PKA-mediated lipolysis.
Suppressed expression of PRIP-1 induces an elevated expression of KCC2 in the spinal cord, resulting in inhibition of nociception and amelioration of neuropathic pain in DKO mice.
PRIP is a novel LC3-binding protein that acts as a negative modulator of autophagosome formation.
The results suggest that PRIP-1 (-/-) mice exhibit the changes of the function and subunits expression of GABA(A) receptor in the spinal cord, which may be responsible for abnormal pain sensation in these mice.
The results suggest that PRIP1 is involved in insulin-induced GABA(A) receptor insertion by recruiting active Akt to the receptor complex.
PRIP-1 plays an important role in regulating the Ins(1,4,5)P3-mediated Ca2+ signaling by modulating type1 inositol polyphosphate 5-phosphatase activity through binding to Ins(1,4,5)P3.
PRIP plays an important role in BDNF-dependent regulation of GABA(A) receptors by mediating the specific association between beta subunits of these receptors with protein phosphatases
Plays an important role in controlling the dynamics of GABAA receptor phosphorylation through protein phosphatase 1 binding.
inositol 1,4,5-trisphosphate binding protein
PLC-L1 , inactive phospholipase C-like protein 1 , phospholipase C related, but catalytically inactive protein , phospholipase C, epsilon , phospholipase C-deleted in lung carcinoma , phospholipase C-related but catalytically inactive protein , phospholipase C, eta 2 pseudogene , 130kDa-Ins(1,4,5)P3 binding protein , PRIP1 , p130