Recombinant Human EPB41 protein (GST tag N-Terminus)
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Recombinant Human EPB41 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 720 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
E41P, EPB41, Protein 4.1, P4.1, 4.1R, Band 4.1, EPB4.1, Erythrocyte membrane protein band 4.1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human EPB41 protein (GST tag N-Terminus) (AB114654)
12.5% SDS-PAGE showing ab114654 at approximately 105.27kDa stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The protein supports cell shape and mechanical properties by linking the cytoskeleton to the plasma membrane. EPB41 is involved in the membrane-cytoskeletal junctional complex where it interacts with other proteins such as spectrin and glycophorin C. This interaction is key in erythrocytes to prevent cell lysis under mechanical stress. Beyond its role in erythrocytes EPB41 assists in protein stabilization and localization within the plasma membrane in other cell types.
Pathways
EPB41 plays an important part in the erythrocyte cell surface structure pathway as well as cell signaling pathways in non-erythroid cells. In the former EPB41 works closely with spectrin and actin to maintain the cellular integrity necessary for oxygen transport. Furthermore in cell signaling pathways its interaction with ankyrin influences membrane organization and signal transduction which are vital for diverse cellular functions.
Specifications
Form
Solid
General info
Function
Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed : 23870127).
Post-translational modifications
Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions.. Phosphorylation on Tyr-660 reduces the ability of 4.1 to promote the assembly of the spectrin/actin/4.1 ternary complex.. O-glycosylated; contains N-acetylglucosamine side chains in the C-terminal domain.
Target data
Product promise
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