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the first report on the transcriptional regulation of hPLSCR4, where Snail (show SNAI1 Proteins) was shown to downregulate the expression of Human phospholipid scramblase 4
biochemical and functional characterization of human phospholipid scramblase 4
Crystallographic analysis of mammalian importin (show KPNA4 Proteins) alpha1 in complex with the hPLSCR4-NLS (show ALDH1A2 Proteins) reveals this minimal NLS (show ALDH1A2 Proteins) binds specifically and exclusively to the minor binding site of importin alpha (show KPNA4 Proteins)
SLPI (show SLPI Proteins) is a ligand for PLSCR1 (show PLSCR1 Proteins) and PLSCR4, which also interact directly with the CD4 receptor at the cell surface of T lymphocytes
Results show that binding affinities of the peptides are in the order hPLSCR1>hPLSCR3>hPLSCR2>hPLSCR4 for Ca2 (show CA2 Proteins)+ and in the order hPLSCR1>hPLSCR2>hPLSCR3>hPLSCR4 for Mg2 (show MUC7 Proteins)+.
Lipopolysaccharide treatment resulted in increased expression of phospholipid scramblase 1(PLSCR-1 (show PLSCR1 Proteins)) and decrease in phospholipid scramblase 4(Plscr4 )messenger RNA demonstrating modulation of PLSCR-1 (show PLSCR1 Proteins) and PLSCR-4 in lipopolysaccharide-induced preterm birth
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.
phospholipid scramblase 4
, Ca(2+)-dependent phospholipid scramblase 4
, PL scramblase 4
, cell growth inhibiting protein 43
, ca(2+)-dependent phospholipid scramblase 4