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study shows that cytoplasmic hereditary spherocytosis mutants cause impaired binding of protein 4.2 to AE1 (show SLC4A1 Proteins), leaving protein 4.2 susceptible to loss during erythrocyte development
Data suggest that one or both of proteins 4.1 and 4.2 cause a portion of band 3 to localize near the spectrin-actin junctions and provide another point of attachment between the membrane skeleton and the lipid bilayer.
spectrin binding domain
Evidence protein 4.2 interacts with the Rh membrane complex member CD47 (show CD47 Proteins) obtained from red cells of patients with hereditary spherocytosis associated with complete protein 4.2 deficiency
protein 4.2 strongly influences CD47 (show CD47 Proteins) levels as well as the extent of membrane skeleton attachment in erythrocytes
The interactions of three protein 4.2-derived recombinant proteins with CDB3 and ankyrin were investigated by using Far-Western blot and pull-down assay.
Data show that a nuclear complex containing TAL1 (show TAL1 Proteins) and LIM (show PDLIM5 Proteins) domain-binding protein Ldb1 (show LDB1 Proteins) transactivates the protein 4.2 (P4.2) gene
Erythrocyte membrane protein band 4.2 is an ATP-binding protein which may regulate the association of protein 3 with ankyrin. It probably has a role in erythrocyte shape and mechanical property regulation. Mutations in the EPB42 gene are associated with recessive spherocytic elliptocytosis and recessively transmitted hereditary hemolytic anemia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, erythrocyte protein 4.2
, erythrocyte surface protein band 4.2
, erythrocyte protein band 4.2
, erythrocyte membrane protein band 4.2