Protein 4.2, also known as Erythrocyte membrane protein band 4.2, is a 691 amino acid transmembrane protein, which possibly regulates mechanical and morphological properties of erythrocytes. Protein 4.2 functions to strongly influence CD47 levels and also regulate the association between Ankyrin and protein 3. Appearing on erythroblasts at a very late stage of red blood cell development, protein 4.2 is predominantly found in liver and is also expressed in spleen, stomach, testis and eye. One of several members of the transglutaminase family, protein 4.2 is subject to a loss of function caused by an amino acid substitution from Cys to Ala in the active site. Complete or partial protein 4.2 absence leads to a weaker than usual association of ankyrin to the membrane skeleton. Defects in the gene encoding protein 4.2 are the cause of hereditary spherocytosis, a hematologic disorder characterized by abnormally shaped erythrocytes and chronic hemolytic anemia. A short and long isoform of protein 4.2 exist as a result of an alternative splicing event. The short isoform is characterized as the major protein 4.2 species in human erythrocyte membranes.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
recommended for detection of protein 4.2 of h and r origin by WB, IP and ELISA: