Recombinant Mouse Multidrug resistance protein 3 (Abcb4), partial

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Product Name Recombinant Mouse Multidrug resistance protein 3 (Abcb4), partial
Description Energy-dependent phospholipid efflux translocator that acts as a positive regulator of biliary lipid secretion. Functions as a floppase that translocates specifically phosphatidylcholine (PC) from the inner to the outer leaflet of the canalicular membrane bilayer into the canaliculi between hepatocytes. Translocation of PC makes the biliary phospholipids available for extraction into the canaliculi lumen by bile salt mixed micelles and therefore protects the biliary tree from the detergent activity of bile salts (PubMed:8106172, PubMed:7912658, PubMed:7592705, PubMed:7814632, PubMed:8725158, PubMed:9366571). Plays a role in the recruitment of phosphatidylcholine (PC), phosphatidylethanolamine (PE) and sphingomyelin (SM) molecules to nonraft membranes and to further enrichment of SM and cholesterol in raft membranes in hepatocytes (By similarity). Required for proper phospholipid bile formation (PubMed:8106172). Indirectly involved in cholesterol efflux activity from hepatocytes into the canalicular lumen in the presence of bile salts in an ATP-dependent manner (PubMed:7814632, PubMed:8725158). May promote biliary phospholipid secretion as canaliculi-containing vesicles from the canalicular plasma membrane (PubMed:9366571). In cooperation with ATP8B1, functions to protect hepatocytes from the deleterious detergent activity of bile salts (PubMed:21820390). Does not confer multidrug resistance (PubMed:1990275)
Synonyms ATP-binding cassette sub-family B member 4Imported
Multidrug resistance protein 21 Publication
Multidrug resistance protein 3By similarity (EC:3.6.3.44)
P-glycoprotein 2By similarity
P-glycoprotein 3By similarity
Host Yeast
Molecular Weight 41.6
Amino Acid Sequence DAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDNIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQTAGSQILSEEFEVELSDEKAAGDVAPNGWKARIFRNSTKKSLKSPHQNRLDEETNELDANVPPVSFLKVLKLNKTEWPYF
Protein Length Cytoplasmic Domain, 352-708aa
Tag N-terminal 6xHis-tagged
Reactivity Mouse
Applications SDS-PAGE
Form Liquid, in Tris-based buffer, 50% glycerol
Purity Greater than 90% as determined by SDS-PAGE.
References "Bile salt-stimulated phospholipid efflux mediated by ABCB4 localized in nonraft membranes."Morita S.Y., Tsuda T., Horikami M., Teraoka R., Kitagawa S., Terada T.J. Lipid Res. 54:1221-1230(2013)
Background Energy-dependent phospholipid efflux translocator that acts as a positive regulator of biliary lipid secretion. Functions as a floppase that translocates specifically phosphatidylcholine (PC) from the inner to the outer leaflet of the canalicular membrane bilayer into the canaliculi between hepatocytes. Translocation of PC makes the biliary phospholipids available for extraction into the canaliculi lumen by bile salt mixed micelles and therefore protects the biliary tree from the detergent activity of bile salts (PubMed:8106172, PubMed:7912658, PubMed:7592705, PubMed:7814632, PubMed:8725158, PubMed:9366571). Plays a role in the recruitment of phosphatidylcholine (PC), phosphatidylethanolamine (PE) and sphingomyelin (SM) molecules to nonraft membranes and to further enrichment of SM and cholesterol in raft membranes in hepatocytes (By similarity). Required for proper phospholipid bile formation (PubMed:8106172). Indirectly involved in cholesterol efflux activity from hepatocytes into the canalicular lumen in the presence of bile salts in an ATP-dependent manner (PubMed:7814632, PubMed:8725158). May promote biliary phospholipid secretion as canaliculi-containing vesicles from the canalicular plasma membrane (PubMed:9366571). In cooperation with ATP8B1, functions to protect hepatocytes from the deleterious detergent activity of bile salts (PubMed:21820390). Does not confer multidrug resistance (PubMed:1990275)
Supplier Cusabio

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