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PITPNM1 belongs to a family of membrane-associated phosphatidylinositol transfer domain-containing proteins that share homology with the Drosophila retinal degeneration B (rdgB) protein (Ocaka et al., 2005. Additionally we are shipping Phosphatidylinositol Transfer Protein, Membrane-Associated 1 Proteins (6) and many more products for this protein.
Showing 10 out of 83 products:
Mouse (Murine) Monoclonal PITPNM1 Primary Antibody for WB - ABIN968719
Aikawa, Hara, Watanabe: Molecular cloning and characterization of mammalian homologues of the Drosophila retinal degeneration B gene. in Biochemical and biophysical research communications 1997
Show all 4 references for ABIN968719
Human Polyclonal PITPNM1 Primary Antibody for WB - ABIN4339780
Aryal, Rao: Deficiency in Cardiolipin Reduces Doxorubicin-Induced Oxidative Stress and Mitochondrial Damage in Human B-Lymphocytes. in PLoS ONE 2016
Cow (Bovine) Polyclonal PITPNM1 Primary Antibody for IF, WB - ABIN374422
Lev, Hernandez, Martinez, Chen, Plowman, Schlessinger: Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. in Molecular and cellular biology 1999
Pitpnm1 null mice showed no hearing defects.
results suggest that Nir2 not only enhances EMT (show ITK Antibodies) in vitro and breast cancer metastasis in animal models, but also contributes to breast cancer progression in human patients.
RdgB homologs play a preemptive role in excluding endogenous and exogenous modified purine deoxyribonucleoside triphosphates (dTNPs) from incorporation into DNA.
Phosphatidic acid production triggers Phosphatidylinositol 4,5-Bisphosphate replenishment mediated by Nir2 and Nir3 (show PITPNM2 Antibodies) at endoplasmic reticulum-plasma membrane junctions.
Nir2 translocates from the Golgi complex to the plasma membrane in response to GF stimulation.
Results suggest a feedback mechanism that replenishes PM PIP2 during receptor-induced Ca(2 (show CA2 Antibodies)+) signaling via the Ca(2 (show CA2 Antibodies)+) effector E-Syt1 (show ESYT1 Antibodies) and the PITP Nir2 at ER-PM junctions.
Nir2, a human homolog of Drosophila melanogaster retinal degeneration B protein (show LEPREL2 Antibodies), is essential for cytokinesis.
A specific Thr (show TRH Antibodies) residue in the Nir2 PI-transfer domain provides a regulatory site for targeting to lipid droplets. This may affect intracellular lipid trafficking & distribution & explain the dominant effect of the RdgB-T59E mutant on retinal degeneration.
Phosphorylation of Nir2 by Cdk1 (show CDK1 Antibodies) facilitates its dissociation from the Golgi apparatus, and phospho-Nir2 is localized in the cleavage furrow and midbody during cytokinesis.
Nir2 is involved in maintaining a critical DAG pool in the Golgi apparatus by regulating its consumption via the CDP (show CUX1 Antibodies)-choline pathway
PITPNM1 belongs to a family of membrane-associated phosphatidylinositol transfer domain-containing proteins that share homology with the Drosophila retinal degeneration B (rdgB) protein (Ocaka et al., 2005
phosphatidylinositol transfer protein, membrane-associated 1
, phosphatidylinositol transfer protein, membrane-associated 1-like
, membrane-associated phosphatidylinositol transfer protein 1-like
, drosophila retinal degeneration B homolog 1
, membrane-associated phosphatidylinositol transfer protein 1
, pyk2 N-terminal domain-interacting receptor 2
, retinal degeneration 9
, PITPnm 1
, PYK2 N-terminal domain-interacting receptor 2
, drosophila retinal degeneration B homolog
, retinal degeneration B alpha 1
, phosphatidylinositol membrane-associated