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Dematin, or EPB49, is an actin-bundling protein originally identified in the erythroid membrane skeleton. Additionally we are shipping erythrocyte Membrane Protein Band 4.9 (Dematin) Kits (5) and erythrocyte Membrane Protein Band 4.9 (Dematin) Proteins (4) and many more products for this protein.
Showing 10 out of 56 products:
Human Polyclonal EPB49 Primary Antibody for EIA, WB - ABIN951882
Vugmeyster, Ostrovsky, Li: Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant. in Journal of biomolecular NMR 2010
Show all 5 references for ABIN951882
Human Polyclonal EPB49 Primary Antibody for ICC, IF - ABIN4304861
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. in Nature methods 2013
Human Polyclonal EPB49 Primary Antibody for IF (p), IHC (p) - ABIN701065
Zhang, Zhao, Chang, Zhang, Chu, Zhang, Liu, Guo, Wang, Gao, Zhang, Chu: Calcium channel blockers ameliorate iron overload-associated hepatic fibrosis by altering iron transport and stellate cell apoptosis. in Toxicology and applied pharmacology 2016
When unphosphorylated, dematin's two F-actin binding domains move independent of one another permitting them to bind different F-actin filaments.
the headpiece domain of dematin regulates calcium mobilization and signaling in platelets
a novel functional role for dematin in regulating erythrocyte membrane function.
Fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin headpiece C-terminal. The reduction of mobility in the loop region upon the S74E mutation can be seen from the (15)N order parameters.
results suggest that phosphorylation of the dematin headpiece acts as a conformational switch within this headpiece domain
a crucial role for this proline residue in structural stability and folding potential of HP (sub)domains consistent with Pro-Trp (show TBPL1 Antibodies) stacking as a more general determinant of protein stability
study investigated motions in the backbone of dematin headpiece domain and its mutant DHPS74E using several complementary NMR relaxation techniques
results suggest that the core domain of dematin exhibits properties typical of a natively unfolded protein, while the headpiece domain is folded in a conformation essentially identical to its native structure
remodeling of the host cell directed Plasmodium includes the recruitment of dematin, an actin-binding protein (show PFN1 Antibodies) of the erythrocyte membrane skeleton and its repositioning to the parasite
physiological significance of dematin and demonstrate a role for the headpiece domain in the maintenance of structural integrity and mechanical properties of erythrocytes in vivo.
Dematin plays an essential role in the maintenance of erythrocyte shape and membrane stability; dematin-membrane interaction could link the junctional complex to the plasma membrane in erythroid cells.
Dematin is expressed in skin, mostly in dermal fibroblasts and hypodermal adipocytes. Knockout mice lacking dematin exhibit hair loss.
These results unveil a new function of dematin as a negative regulator of the RhoA (show RHOA Antibodies) activation pathway with physiological implications for normal and pathogenic signaling pathways.
Dematin, or EPB49, is an actin-bundling protein originally identified in the erythroid membrane skeleton. Its actin-bundling activity is abolished upon phosphorylation by cAMP-dependent protein kinase and is restored after dephosphorylation (Rana et al., 1993
erythrocyte membrane protein band 4.9 (dematin)
, dematin actin-binding protein
, erythrocyte membrane protein band 4.9
, erythrocyte protein band 4.9