Tenidap is an anti-inflammatory and anti-rheumatic with a variety of activities. Tenidap preferentially inhibits COX-1 with an IC50 value of 30 nM, and also has some lesser inhibitory activity towards COX-2 and 5-lipoxygenase (IC50 values are 1.2 and > 30 μM for COX-2 and 5-lipoxygenase respectively). Tenidap is also a cytokine modulator, an opener of inward rectifying hKIR2.3 channels (EC50 = 402 nM) and has been shown to modulate cytoplasmic pH and inhibit anion transport in vitro.
Tenidap is an anti-inflammatory, anti-rheumatic and cytokine modulator.
The Journal of rheumatology, 27(4), 888-893 (2000-04-27)
To demonstrate that serum matrix metalloproteinase-3 (MMP-3) is a variable associated with disease activity and with the response to treatment in rheumatoid arthritis (RA). Serum MMP-3 levels were measured and compared to biological and clinical disease activity variables in 20
We have compared the formation of pores in rat submandibular acinar cells in response to 2',3'-O-(4-benzoylbenzoyl) adenosine 5'-triphosphate (Bz-ATP) and maitotoxin. Bz-ATP (100 microM) permeabilized the cells to ethidium bromide. The uptake of ethidium increased to 29+/-1% of maximal uptake
Pflugers Archiv : European journal of physiology, 442(5), 709-717 (2001-08-21)
In the present experiments we expressed the rat kidney Na+-HCO3- cotransporter (rkNBC) in Xenopus laevis oocytes to reinvestigate the flux coupling ratio under improved measuring conditions. Essentially the current/voltage (I/V) relationship of isolated inside-out giant membrane patches was measured and
European journal of pharmacology, 355(2-3), 235-244 (1998-10-06)
Tenidap is an anti-inflammatory drug whose mechanism of action is not fully understood. It has been shown to block plasma membrane anion transport and to decrease release of interleukin-1beta, probably via the inhibition of interleukin-1beta converting enzyme. In the present
American journal of physiology. Cell physiology, 292(5), C1787-C1798 (2007-01-26)
Others have shown that H(2)DIDS reversibly and covalently binds to the first lysine (K) in the SKLIK motif at the extracellular end of transmembrane segment 5 of the Cl-HCO(3) exchanger AE1. Here we mutated K558, K559, and/or K562 in the
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