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anti-Human PIGA Antibodies:
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Cow (Bovine) Polyclonal PIGA Primary Antibody for WB - ABIN2782189
Traulsen, Pacheco, Dingli: On the origin of multiple mutant clones in paroxysmal nocturnal hemoglobinuria. in Stem cells (Dayton, Ohio) 2007
The study established a human induced pluripotent stem cell (hiPSC) model containing the PIGAc.1234C>T mutation to study the effects of a hypomorphic allele of PIGA on neuronal development. Neuronal differentiation from neural progenitor cells generated by embryoid bodie formation in PIGAc.1234C>T is significantly impaired with decreased proliferation, aberrant synapse formation and abnormal membrane depolarization.
Pig-a MFs as measured by the RBC (show CACNA1C Antibodies) Pig-a assay for the ENU-treated group increased in a time-dependent manner with the maximum value at week 4; however, those using the PIGRET assay reached comparable values at week 1
A recurrent germline mutation in the PIGA gene causes Simpson-Golabi-Behmel syndrome type 2.
This case reports on a new missense PIGA germline mutation in a Chinese male infant presenting with developmental arrest and multisystemic disorders.
the PIGA mutation in this family likely causes a reduction in GPI (show GNPDA1 Antibodies) anchor protein (show CELSR3 Antibodies) cell surface expression in various cell types, resulting in the observed pleiotropic phenotype involving central nervous system, skin, and iron metabolism.
Our data strongly suggest that the early frameshift mutation in PIGA produces a truncated hypomorph, which is sufficient to rescue the lethality in males but not the MCAHS2-like phenotype.
The results of this study confirmed that PIGA mutations are one genetic cause of early-onset epileptic encephalopathies, suggesting that GPI (show GNPDA1 Antibodies)-anchor deficiencies may be an underlying cause of EOEE.
The small population of PIG-A mutant cells in myelodysplastic syndromes do not arise from multipotent hematopoietic stem cells.
An X chromosome exome next-generation sequencing screen identified a single nonsense PIGA mutation.
loss of PIG-A or a combination of genes within the 0.5 Mb commonly deleted region leads to a phenotype capable of avoiding immune surveillance, but is not inherently malignant.
Diet-induced obesity increases the frequency of Pig-a mutant erythrocytes in male C57BL/6J mice.
Single cell gel electrophoresis (SCGE (show SGCE Antibodies)) and Pig-a mutation assay in vivo-tools for genotoxicity testing from a regulatory perspective: a study of benzo[a]pyrene in Ogg1 (show OGG1 Antibodies)(-/-) mice.
Reduced IgE/antigen-mediated passive cutaneous anaphylaxis is detected in mice with Piga-deficient mast cells.
Deletion of the Pig-a gene in hematopoietic cells does not cause frank marrow failure but leads to the appearance of clonally-restricted, inactive yet functionally competent CD8 (show CD8A Antibodies) T cells.
Piga gene mutation does not alter susceptibility to cell death in thymocytes, granulocytes, and hematopoietic progenitor cells.
Pig-a-knockout females are infertile, and eggs recovered from the females after mating are unfertilized.
processing profilaggrin (show FLG Antibodies) to its monomeric form was impaired in Pig-a null mouse epidermis
Piga expression is required to properly orient hair cells in the inner ear, a process regulated by the planar cell polarity pathway.
This gene encodes a protein required for synthesis of N-acetylglucosaminyl phosphatidylinositol (GlcNAc-PI), the first intermediate in the biosynthetic pathway of GPI anchor. The GPI anchor is a glycolipid found on many blood cells and which serves to anchor proteins to the cell surface. Paroxysmal nocturnal hemoglobinuria, an acquired hematologic disorder, has been shown to result from mutations in this gene. Alternate splice variants have been characterized. A related pseudogene is located on chromosome 12.
N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein
, phosphatidylinositol glycan anchor biosynthesis, class A (paroxysmal nocturnal hemoglobinuria)
, phosphatidylinositol glycan, class A (paroxysmal nocturnal hemoglobinuria)
, GLCNAC-PI synthesis protein
, GPI anchor biosynthesis
, class A GlcNAc-inositol phospholipid assembly protein
, phosphatidylinositol N-acetylglucosaminyltransferase subunit A
, phosphatidylinositol-glycan biosynthesis, class A protein
, glcNAc-PI synthesis protein
, phosphatidylinositol glycan, class A
, phosphatidylinositol-glycan biosynthesis class A protein
, phosphatidylinositolglycan class A