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The protein encoded by EPB41, together with spectrin and actin, constitute the red cell membrane cytoskeletal network. Zusätzlich bieten wir Ihnen Erythrocyte Membrane Protein Band 4.1 (Elliptocytosis 1, RH-Linked) Proteine (8) und Erythrocyte Membrane Protein Band 4.1 (Elliptocytosis 1, RH-Linked) Kits (5) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal EPB41 Primary Antibody für ELISA, WB - ABIN560751
Ciana, Achilli, Balduini, Minetti: On the association of lipid rafts to the spectrin skeleton in human erythrocytes. in Biochimica et biophysica acta 2010
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Our study shows alternative polyadenylation to be an additional mechanism for the generation of 4.1 protein diversity in the already complex EPB41-related genes. Understanding the diversity of EPB41 RNA processing is essential for a full appreciation of the many 4.1 proteins expressed in normal and pathological tissues.
identification of EPB41 as a hepatocellular carcinoma susceptibility gene in vitro and in vivo; consistent with this notion, EPB41 expression is significantly decreased in HCC (zeige FAM126A Antikörper) tissue specimens, especially in portal vein metastasis or intrahepatic metastasis, compared to normal tissues
The 4.1R, 4.1N (zeige EPB41L1 Antikörper) and 4.1B (zeige EPB41L3 Antikörper) are all expressed at the lateral membrane as well as cytoplasm of epithelial cells, suggesting a potentially redundant role of these proteins.
Calcium mediates the conformation-based 4.1R FERM domain binding to membrane proteins by calmodulin.
Results suggest a previously unidentified role for the scaffolding protein 4.1R in locally controlling CLASP2 (zeige CLASP2 Antikörper) behavior, CLASP2 (zeige CLASP2 Antikörper) cortical platform turnover and GSK3 (zeige GSK3b Antikörper) activity, enabling correct MT organization and dynamics essential for cell polarity.
We conclude that PIP2 may play an important role as a modulator of apo (zeige C9orf3 Antikörper)-CaM binding to 4.1R(80) throughout evolution.
Plasmodium falciparum PF3D7_0402000 was identified as a new binding partner for the major erythrocyte cytoskeletal protein (zeige ACTN1 Antikörper), 4.1R.
a novel gene region, EPB41, which may be associated with smoking cessation, along with gene regions in CNR1 (zeige CNR1 Antikörper) that may be targeted to further elucidate the etiology of gender differences in smoking behaviors.
4.1R regulates NHE1 (zeige SLC9A1 Antikörper) activity through a direct protein-protein interaction that can be modulated by intracellular pH and Na(+) and Ca(2 (zeige CA2 Antikörper)+) concentrations.
Further studies involving siRNA-mediated knockdowns of spectrin, adducin, or p4.1 revealed that those proteins are needed for efficient docking of enterohaemorrhagic Escherichia coli to host cells.
Data hypothesize that protein 4.1 (4.1R) could function as a linker protein (zeige LAT Antikörper) between cytokeratin (zeige KRT1 Antikörper) and the actin-based cytoskeleton.
4.1G interacts with a subset of CNG (zeige CNGA1 Antikörper) channels and implicate this protein-protein interaction in organizing the spatial arrangement of CNG (zeige CNGA1 Antikörper) channels in the plasma membrane of retinal outer segments.
Band 4.1 protein is found in a retinal cDNA library screened for proteins interacting with the intracellular C-terminus of the metabotropic glutamate (zeige GRIN2A Antikörper) receptor isoform 8a (mGluR8a).
This suggests that 4.1R may influence myogenesis by preventing VHL (zeige VHL Antikörper)-mediated myogenin (zeige MYOG Antikörper) degradation.
The proportion of 4.1R-positive cells was significantly higher in the HF group than in the controls, which was confirmed by the positive mRNA expression of 4.1R. 4.1R localized mostly to the plasma membrane of myocardial cells and was upregulated with the progression of HF. This suggests that 4.1R may be associated with HF progression.
suggest that 4.1R can prevent pathogenic autoimmunity in MS/EAE progression by suppressing the CD4 (zeige CD4 Antikörper)(+) T cell activation
Loss of 4.1/NuMA (zeige NUMA1 Antikörper) interaction results in spindle orientation defects and inhibition of Cdk1 (zeige CDK1 Antikörper) causes increase in cortical NuMA (zeige NUMA1 Antikörper) localization
a functional role for 4.1R in small intestinal calcium absorption through regulation of membrane expression of PMCA1b (zeige ATP2B1 Antikörper).
At the intercalated disc 4.1R does not colocalise with the adherens junction protein, beta-catenin (zeige CTNNB1 Antikörper), but does overlap with the other plasma membrane signalling proteins, the Na/K-ATPase (zeige ATP1A1 Antikörper) and the Na/Ca exchanger NCX1 (zeige SLC8A1 Antikörper).
Cell adhesion and signaling pathways regulated by alphavbeta8 integrin and Band 4.1B (zeige EPB41L3 Antikörper) are essential for normal formation and function of the heart during embryogenesis.
A conserved exonic splicing silencer element (CE(16)) in protein 4.1R exon 16 (E16 (zeige SLC7A5 Antikörper)) interacts with hnRNP A/B (zeige HNRNPAB Antikörper) proteins & plays a role in repression of E16 (zeige SLC7A5 Antikörper) splicing during early erythropoiesis
We speculate that over the repetitive cycles of heart muscle contraction and relaxation, 4.1R is likely to locate, support, and coordinate functioning of key membrane-bound macromolecular assemblies.[Epb41]
These results suggest that erythroid protein 4.1 plays a major role in volume regulation and physiologically downregulates Na/H exchange in mouse erythrocytes.
The protein encoded by this gene, together with spectrin and actin, constitute the red cell membrane cytoskeletal network. This complex plays a critical role in erythrocyte shape and deformability. Mutations in this gene are associated with type 1 elliptocytosis (EL1). Alternatively spliced transcript variants encoding different isoforms have been described for this gene.
erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)
, protein 4.1R
, cytoskeletal protein 4.1
, protein 4.1
, protein 4.1-like
, band 4.1
, erythrocyte surface protein band 4.1
, erythroid membrane skeletal protein 4.1
, erythroid protein 4.1