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The protein encoded by EPB41, together with spectrin and actin, constitute the red cell membrane cytoskeletal network. Additionally we are shipping Erythrocyte Membrane Protein Band 4.1 (Elliptocytosis 1, RH-Linked) Antibodies (63) and Erythrocyte Membrane Protein Band 4.1 (Elliptocytosis 1, RH-Linked) Kits (5) and many more products for this protein.
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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 (show FAM126A Proteins) tissue specimens, especially in portal vein metastasis or intrahepatic metastasis, compared to normal tissues
The 4.1R, 4.1N (show EPB41L1 Proteins) and 4.1B (show EPB41L3 Proteins) 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 behavior, CLASP2 cortical platform turnover and GSK3 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 (show C9orf3 Proteins)-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 (show ACTN1 Proteins), 4.1R.
a novel gene region, EPB41, which may be associated with smoking cessation, along with gene regions in CNR1 (show CNR1 Proteins) that may be targeted to further elucidate the etiology of gender differences in smoking behaviors.
4.1R regulates NHE1 (show SLC9A1 Proteins) activity through a direct protein-protein interaction that can be modulated by intracellular pH and Na(+) and Ca(2 (show CA2 Proteins)+) 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 (show LAT Proteins) between cytokeratin (show KRT1 Proteins) and the actin-based cytoskeleton.
4.1G interacts with a subset of CNG (show CNGA1 Proteins) channels and implicate this protein-protein interaction in organizing the spatial arrangement of CNG (show CNGA1 Proteins) 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 (show GRIN2A Proteins) receptor isoform 8a (mGluR8a).
This suggests that 4.1R may influence myogenesis by preventing VHL (show VHL Proteins)-mediated myogenin (show MYOG Proteins) 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 (show CD4 Proteins)(+) T cell activation
Loss of 4.1/NuMA interaction results in spindle orientation defects and inhibition of Cdk1 causes increase in cortical NuMA localization
a functional role for 4.1R in small intestinal calcium absorption through regulation of membrane expression of PMCA1b (show ATP2B1 Proteins).
At the intercalated disc 4.1R does not colocalise with the adherens junction protein, beta-catenin (show CTNNB1 Proteins), but does overlap with the other plasma membrane signalling proteins, the Na/K-ATPase (show ATP1A1 Proteins) and the Na/Ca exchanger NCX1 (show SLC8A1 Proteins).
Cell adhesion and signaling pathways regulated by alphavbeta8 integrin and Band 4.1B (show EPB41L3 Proteins) 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) interacts with hnRNP A/B proteins & plays a role in repression of E16 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