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Quality Level
Assay
≥98% (HPLC)
form
powder
storage condition
desiccated
color
white to beige
solubility
DMSO: 2 mg/mL, clear
storage temp.
−20°C
InChI
1S/C14H18Cl3N5O2.ClH/c1-14(2)21-12(18)20-13(19)22(14)24-5-3-4-23-11-7-9(16)8(15)6-10(11)17;/h6-7H,3-5H2,1-2H3,(H4,18,19,20,21);1H
InChI key
VOTSDCGUYAGUNS-UHFFFAOYSA-N
Biochem/physiol Actions
WR99210 is a potent inhibitor of Plasmodium falciparum dihydrofolate reductase (pfDHFR), which is a major malarial drug target. It has subnanomolar potency for the wild type, double mutant and quadruple mutant dihydrofolate reductases.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Experimental parasitology, 87(3), 222-228 (1997-11-26)
With emerging drug resistance in Plasmodium falciparum, novel antifolates effective against pyrimethamine-resistant and cycloguanil-resistant dihydrofolate reductase (DHFR) are in demand. Based on structural similarity to cycloguanil, it has been proposed that WR99210, and its metabolic precursor PS-15, exerts selective antimalarial
Cellular microbiology, 22(2), e13123-e13123 (2019-10-28)
A hallmark of the biology of Plasmodium falciparum blood stage parasites is their extensive host cell remodelling, facilitated by parasite proteins that are exported into the erythrocyte. Although this area has received extensive attention, only a few exported parasite proteins
Molecular and biochemical parasitology, 238, 111292-111292 (2020-06-09)
Defining protein-protein interactions is fundamental to the understanding of gene function. Protein-fragment complementation assays have been used for the analysis of protein-protein interactions in various organisms. The split-dihydrofolate reductase (DHFR) protein-fragment complementation assay utilises two complementary fragments of the enzyme
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