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An N-acyl amide that uncouples mitochondrial respiration independent of UCP1 in vitro; decreases body weight and food intake, preferentially decreasing fat mass in a diet-induced obesity mouse model; improves glucose homeostasis and increases energy expenditure while slightly decreasing overall locomotor activity
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Mismatch Endonuclease I is a Mg2 dependent DNA endonuclease that specifically cleaves mismatched base pairs (TT GG and TG mismatches). Mismatch Endonuclease I cleaves the 3rd phosphodiester bond on the 5 side of the mismatched base in both strands leaving a 5 bp overhang. While Mismatch Endonuclease I prefers to cleave TT GG and TG DNA mismatches it will also readily cleave TI GI and GU DNA mismatches. Additionally Mismatch Endonuclease I has been shown to nick the thymine containing strand of TC DNA mismatches and cleave TG and TU (DNARNA) mismatches albeit to a lesser extent than DNADNA mismatches.
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A fluorogenic substrate for vanin-1; AMC is released upon enzymatic cleavage by vanin-1 and its fluorescence can be used to quantify vanin-1 activity; ex/em = 340-360/440-460 nm, respectively
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A fluorogenic peptide substrate; used to assess the activity of bacterial proteases from P. aeruginosa and S. aureus; enzyme activity can be quantified by fluorescent detection of free AMC (also known as 7-amino-4-methylcoumarin), which is excited at 340-360 nm and emits at 440-460 nm
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A PDGFR and FGFR inhibitor (IC50s 5.35 4.6 28 28 and 78 nM for PDGFRa PDGFRB FGFR1 -2 and -3 respectively) selective for these kinases over FGFR4 (IC50 >1000 nM) but also inhibits c-Kit VEGFR2 VEGFR1 and IGF-1R (IC50s 67 33 36 and 75 nM respectively) as well as EGFR BTK Cdk4/cyclin D3 and MET (IC50s 128 198 214 and 396 nM respectively) inhibits the proliferation of MG-63 U2OS MNNG/HOS and Saos-2 cells (IC50s 0.84 0.76 1.36 and 0.72 UM respectively) inhibits the migration and invasion of U87MG and LN-229 cells at 0.3 and 0.5 UM decreases tumor volume and increases survival in a U87MG orthotopic mouse xenograft model 30 mg/kg
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Prepared by a method developed at Worthington in which native, double-stranded calf thymus DNA is covalently bound to cellulose. Suitable for the purification of many DNA binding proteins such as polymerases, transcription factors, and terminators, etc.
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