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Data indicate heterogeneous expression of phospholipid scramblase 1 (PLSCR1) and suggest its possible implication in the response to anticancer therapies, especially to drugs promoting protective autophagy.
Human phospholipid scramblase 1 has five histidine residues and point mutations of histidine residues to alanine in hPLSCR1 resulted in 60 % loss in nuclease (show DCLRE1C Proteins) activity.
directed mutagenesis revealed the importance of c-Myc (show MYC Proteins) binding sites from -751 to -756 and -548 to -553 on the promoter of hPLSCR1in transcriptionally regulating the expression of hPLSCR1.
PLSCR1 positively regulates hepatic carcinoma cell proliferation and migration through interacting with midkine (show MDK Proteins)
Suggest role for PLSCR1 in negatively regulating trophoblast fusion rather than directly promoting fusion.
PLSCR1 mediates the antiviral activity and anticarcinogenesis against hepatitis B virus by regulating HBx stability.
affinity of SCR for cholesterol-rich domains in membranes
The C-terminal transmembrane domain of human phospholipid scramblase 1 is essential for the protein flip-flop activity and Ca(2 (show CA2 Proteins))-binding.
This is the first report showing the transcriptional regulation of hPLSCR1 expression by Snail (show SNAI1 Proteins) TF and its possible implications in cancer progression.
PLSCR1 interacted with ANG (show ANG Proteins) in the cell nucleus and regulated rRNA transcription.
PLSCR1 aggravates anaphylactic reactions by increasing Fc epsion RI-dependent mast cell degranulation.
Genetic knockdown of PLSCR1 activity reduces intracellular calcium dysregulation, prevents phosphatidylserine externalization, and enables months-long protection of vector-transduced, transgene-expressing cells from microglial phagocytosis.
Phospholipid scramblase 1 regulates phosphatidylserine exposure in response to oxygen stress, leading to beta2-glycoprotein I and IgM binding and lipid-mediated, inflammatory responses.
Lipopolysaccharide treatment resulted in increased expression of phospholipid scramblase 1(PLSCR-1) and decrease in phospholipid scramblase 4(Plscr4 (show PLSCR4 Proteins) )messenger RNA demonstrating modulation of PLSCR-1 and PLSCR-4 (show PLSCR4 Proteins) in lipopolysaccharide-induced preterm birth
Study demonstrates that PLSCR1 is a TLR9 (show TLR9 Proteins)-interacting protein that plays an important role in pDC's type 1 IFN responses by regulating TLR9 (show TLR9 Proteins) trafficking to the endosomal compartment.
the capacity of PLSCR1 to augment G-CSF (show CSF3 Proteins)-dependent production of mature neutrophils from myeloid progenitors is unrelated to its reported activities at the endofacial surface of the plasma membrane but does require entry of the protein into the nucleus
PLSCR1 appears to influence progression of UV-induced apoptosis and could be a point of regulation or intervention during programmed cell death
PLSCR1, which is itself an IFN-stimulated gene-encoded protein, provides a mechanism for amplifying and enhancing the IFN response through increased expression of a select subset of potent antiviral genes
PLSCR1 binds to the promoter region of the IP3R1 (show ITPR1 Proteins) gene to enhance its expression
These findings demonstrate a functional interdependence between onzin and PLSCR1.
may act as a downstream mediator of immune response in IgE receptor signaling\; may transport phospholipids in the plasma membrane
phospholipid scramblase 1
, PL scramblase 1
, ca(2+)-dependent phospholipid scramblase 1
, phospholipid scramblase 2
, erythrocyte phospholipid scramblase
, transplantability-associated protein 1
, PL scramblase 2
, ca(2+)-dependent phospholipid scramblase 2