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ABCB11 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O95342 |
|---|---|
| Clone Names | 2092003 |
| Gene ID | 8647 |
|---|---|
| Other Names | Bile salt export pump, ATP-binding cassette sub-family B member 11, ABCB11, BSEP |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6110a was selected from the C-term region of human ABCB11 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | ABCB11 (HGNC:42) |
|---|---|
| Synonyms | BSEP {ECO:0000303|Ref.2} |
| Function | Catalyzes the transport of the major hydrophobic bile salts, such as taurine and glycine-conjugated cholic acid across the canalicular membrane of hepatocytes in an ATP-dependent manner, therefore participates in hepatic bile acid homeostasis and consequently to lipid homeostasis through regulation of biliary lipid secretion in a bile salts dependent manner (PubMed:16332456, PubMed:22262466, PubMed:15791618, PubMed:18985798, PubMed:19228692, PubMed:20398791, PubMed:24711118, PubMed:29507376, PubMed:20010382, PubMed:32203132). Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts (PubMed:16332456). Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion (PubMed:15901796, PubMed:18245269). |
| Cellular Location | Apical cell membrane; Multi-pass membrane protein. Recycling endosome membrane {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O70127}. Endosome {ECO:0000250|UniProtKB:O70127}. Cell membrane; Multi-pass membrane protein. Note=Internalized at the canalicular membrane through interaction with the adapter protein complex 2 (AP-2) (PubMed:22262466). At steady state, localizes in the canalicular membrane but is also present in recycling endosomes. ABCB11 constantly and rapidly exchanges between the two sites through tubulo-vesicles carriers that move along microtubules. Microtubule-dependent trafficking of ABCB11 is enhanced by taurocholate and cAMP and regulated by STK11 through a PKA-mediated pathway. Trafficking of newly synthesized ABCB11 through endosomal compartment to the bile canalicular membrane is accelerated by cAMP but not by taurocholate (By similarity). Cell membrane expression is up-regulated by short- and medium-chain fatty acids (PubMed:20398791) {ECO:0000250|UniProtKB:O70127, ECO:0000269|PubMed:20398791, ECO:0000269|PubMed:22262466} |
| Tissue Location | Expressed predominantly, if not exclusively in the liver, where it was further localized to the canalicular microvilli and to subcanalicular vesicles of the hepatocytes by in situ |
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Provided below are standard protocols that you may find useful for product applications.
Background
ABCB11 is involved in the ATP-dependent secretion of bile salts into the canaliculus of hepatocytes. It is expressed predominatly, if not exclusively, in the liver, where it is further localized to the canilicular microvilli and to subcanilicular vesicles fo the hepatocytes. Structurally, ABCB11 is a multifunctional polypeptide with two homologus halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain. Defects in ABCB11 are the cause of progressive familial intrahepatic cholestasis 2 (PFIC2). PFIC2 is an inherited liver disease of childhood which is characterized by cholestasis and normal serum gamma-glutamyltransferase activity. Defects in ABCB11 are also found in cases of chronic intrahepatic cholestasis without obvious familial history of chronic liver disease.
References
Chen, H.L., et al., J. Pediatr. 140(1):119-124 (2002).Saito, S., et al., J. Hum. Genet. 47(1):38-50 (2002).Strautnieks, S.S., et al., Nat. Genet. 20(3):233-238 (1998).
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