AOAH Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P28039 |
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Clone Names | 110617045 |
Gene ID | 313 |
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Other Names | Acyloxyacyl hydrolase, Acyloxyacyl hydrolase small subunit, Acyloxyacyl hydrolase large subunit, AOAH |
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 | AOAH {ECO:0000303|PubMed:1883828} |
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Function | Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (PubMed:1883828, PubMed:8089145, PubMed:29343645). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (By similarity). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (By similarity). |
Cellular Location | Secreted. Cytoplasmic vesicle. Note=Detected in urine {ECO:0000250|UniProtKB:O35298} |
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Provided below are standard protocols that you may find useful for product applications.
Background
This locus encodes both the light and heavy subunits ofacyloxyacyl hydrolase. The encoded enzyme catalyzes the hydrolysisof acyloxylacyl-linked fatty acyl chains from bacteriallipopolysaccharides, effectively detoxifying these molecules. Theencoded protein may play a role in modulating host inflammatoryresponse to gram-negative bacteria. Alternatively splicedtranscript variants have been described.
References
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Pelak, K., et al. J. Infect. Dis. 201(8):1141-1149(2010)Barnes, K.C., et al. J. Allergy Clin. Immunol. 118(1):70-77(2006)Coulthard, M.G., et al. Infect. Immun. 64(5):1510-1515(1996)Staab, J.F., et al. J. Biol. Chem. 269(38):23736-23742(1994)
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