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Human Polyclonal EPB42 Primary Antibody für WB - ABIN515322
Hammill, Risinger, Joiner, Keddache, Kalfa: Compound heterozygosity for two novel mutations in the erythrocyte protein 4.2 gene causing spherocytosis in a Caucasian patient. in British journal of haematology 2011
study shows that cytoplasmic hereditary spherocytosis mutants cause impaired binding of protein 4.2 to AE1 (zeige SLC4A1 Antikörper), 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 (zeige CD47 Antikörper) obtained from red cells of patients with hereditary spherocytosis associated with complete protein 4.2 deficiency
protein 4.2 strongly influences CD47 (zeige CD47 Antikörper) 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 (zeige TAL1 Antikörper) and LIM (zeige PDLIM5 Antikörper) domain-binding protein Ldb1 (zeige LDB1 Antikörper) 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