ABCB9 Antibody

1. The structure of the unique domain of TAPL, is reported. PMID: 24013930
2. LAMP proteins retain TAPL on the limiting membrane of endosomes and prevent its sorting to intraluminal vesicles. PMID: 22641697
3. These results suggest that TAPL may be localized to the microdomains (lipid rafts) of lysosomal membranes enriched in cholesterol. PMID: 21212514
4. By dissecting ABCB9, distinct functions were assigned to the core complex and the extra N-terminal transmembrane domain. PMID: 20377823
5. is part of the peptide-loading complex in the classic route of antigen processing via major histocompatibility complex class I molecules PMID: 15863492
6. These findings suggest that the transport activity of hTAPL is important for conferring high valinomycin-sensitive phenotype to yeast. PMID: 16554024
7. the TAPL-specific translocation of peptides into isolated lysosomes strictly requires ATP hydrolysis PMID: 17977821
8. The ATP-binding of TAPL required Mg(2+), and was observed at neutral pH. Chemical cross-linking experiments suggested that TAPL forms a homodimer in the membrane and under the solubilized conditions. PMID: 18175933
9. analysis of lipid activation of the lysosomal transport complex ABCB9 PMID: 18434309
10. These results suggest that the sorting signal for lysosomes is present within the amino-terminal transmembrane domain (Met(1)-Arg(141)) of the TAPL molecule. PMID: 18952056

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HGNC: 50

OMIM: 605453

KEGG: hsa:23457

STRING: 9606.ENSP00000280560

UniGene: Hs.511951