FPR A14 - CAS 329691-12-5
Category: Inhibitor
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Molecular Formula:
C23H20N2O5
Molecular Weight:
404.42
COA:
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Targets:
Others
Description:
FPR A14 is a formyl peptide receptor (FPR) agonist that potently activates neutrophils in vitro (EC50 = 42 and 630 nM for neutrophil chemotaxis and Ca2+ mobilization, respectively).
Brife Description:
FPR agonist
Purity:
≥99% by HPLC
Synonyms:
AG 14; AG14; AG-14; 1,3-Benzodioxolane-5-carboxylic acid 4'-benzyloxy-3'-methoxybenzylidene hydrazide
MSDS:
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InChIKey:
ULOKADSYVZOTTL-CFRMEGHHSA-N
InChI:
InChI=1S/C23H20N2O5/c1-27-21-11-17(7-9-19(21)28-14-16-5-3-2-4-6-16)13-24-25-23(26)18-8-10-20-22(12-18)30-15-29-20/h2-13H,14-15H2,1H3,(H,25,26)/b24-13-
Canonical SMILES:
COC1=C(C=CC(=C1)C=NNC(=O)C2=CC3=C(C=C2)OCO3)OCC4=CC=CC=C4
1.Effects of NH4+ and K+ on the energy metabolism in Sp2/0-Ag14 myeloma cells.
Martinelle K;Häggström L Cytotechnology. 1999 Jan;29(1):45-53. doi: 10.1023/A:1008084622991.
Potassium ions decrease the transport rate of ammonium ions into myeloma and hybridoma cells, one effect of the involved transport processes being an increased energy demand (Martinelle and Häggström, 1993; Martinelle et al., 1998b). Therefore, the effects of K+ and NH4+ on the energy metabolism of the murine myeloma cell line, Sp2/0-Ag14, were investigated. Addition of NH4Cl (10 mM) increased the metabolism via the alanine transaminase (alaTA) pathway, without increasing the consumption of glutamine. As judged by the alanine production, the energy formation from glutamine increased by 155%. The presence of elevated concentrations of KCl (10 mM) was positive, resulting in a decreased uptake of glutamine (45%), and an even larger suppression of ammonium ion formation (70%), while the same throughput via the alaTA pathway (and energy production from glutamine) was retained as in the control culture. However, the simultaneous presence of 10 mM K+ and 10 mM NH4+ was more inhibitory than NH4Cl alone; an effect that could not be ascribed to increased osmolarity. Although the culture with both K+ and NH4+ consumed 60% more glutamine than the culture with NH4+ alone, the energy generation from glutamine could not be increased further, due to the suppression of the glutamate dehydrogenase pathway.
2.Anti-TNP monoclonal antibodies as reagents for enzyme immunoassay (ELISA).
Léo P;Ucelli P;Augusto EF;Oliveira MS;Tamashiro WM Hybridoma. 2000 Dec;19(6):473-9.
The aim of this study was to produce anti-TNP monoclonal antibodies (MAbs) that could be conjugated and used for the detection of antigen-antibody reactions, in which the antigen specific-antibody had been previously bound to trinitrophenyl (TNP). For hybridoma production, SP2/0-Ag14 cells were fused with spleen cells from mice previously immunized with TNP-ovalbumin (TNP-OVA). After 10 days, enzyme-linked immunoadsorbent assay (ELISA) was used to detect anti-TNP antibodies in the supernatants, and five cultures were found to be strictly positive for TNP. Three of these were subsequently cloned by limiting dilution, and 15 clones were chosen for expansion based on the criterion of high reactivity against TNP. Anti-TNP MAbs produced by those clones were isotyped as IgG1, and purified by Sepharose-protein G affinity cromatography from ascites developed in BALB/c mice. Two purified MAbs (1B2.1B6 and 1B2.1E12) were coupled to horseradish peroxidase (HRPO). The resulting conjugates were evaluated in ELISA tests for interferon-gamma and interleukin-4 detection, in which the secondary anti-cytokine antibodies were coupled either to TNP or biotin. The performance of anti-TNP conjugates in these assays were compared with a biotin-streptavidin/peroxidase system.
3.Cross-species reactivity of a monoclonal antibody against glutathione S-transferase fusion protein of human beta 2-adrenergic receptor.
Shin CY;Kang SJ;Song MR;Park KH;Seo DO;Cheong JH;Ko KH Biochem Mol Biol Int. 1998 Jun;45(2):215-25.
The purpose of the present study was to produce and characterize a monoclonal antibody against human beta 2-adrenergic receptor. Male BALB/c mice were immunized with glutathione S-transferase (GST) fusion protein of the C-terminal portion of the human beta 2-adrenergic receptor which was expressed in E.Coli. The immunized splenocytes were fused with myeloma SP2/0-Ag14 cells and the resulting monoclonal antibody was named as mAb beta C02. The monoclonal antibody beta C02 was determined as IgM subtype and then purified by anti-mouse IgM-agarose affinity chromatography. The results of ELISA, Western blot, and immunocytochemistry showed that mAb beta C02 recognized human beta 2-adrenergic receptor in the beta 2-adrenergic receptor-GST fusion protein and human epidermoid carcinoma cell line A431 with highly specific immunoreactivity. In addition, mAb beta C02 showed cross-species reactivity against beta-adrenergic receptor of hamster lung and rat brain as revealed by Western blot and immunohistochemistry. The monoclonal antibody beta C02 may provide useful tools for the study of the beta-adrenergic receptor of human and other species including rats.
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CAS 329691-12-5 FPR A14

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