Recombinant Human ALIX Protein

重组人Alix蛋白 | 重组人ALG-2相互作用蛋白X蛋白

AIP1 | ALG 2 interacting protein 1 | ALG-2-interacting protein 1 | ALG2 interacting protein X | Alix | Apoptosis linked gene 2 interacting protein X | Dopamine receptor interacting protein 4 | DRIP4 | Hp95 | KIAA1375 | MGC17003 | PDC6I_HUMAN | PDCD6 inter

rp214499-10μg

10μg

无载体

≥95%(SDS-PAGE)

Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Appears to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function implies the interaction with CHMP4B. May play a role in the regulation of both apoptosis and cell proliferation. Post-translational: May be phosphorylated on tyrosine residues by activated PDGFRB.

重组表达

19.3 kDa

N-His

17.2 kDa, under reducing conditions; 17.8 & 37.4 kDa, under non-reducing conditions.

E. coli Accession #: Q8WUM4 | E. coli

<1.0 EU/μg

人(Human)

559-718 aa

MHHHHHHATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNVPISQKFTDLFEKMVPVSVQQSLAAYNQRKADLVNRSIAQMREATTLA

No

Yes