Binds to an extracellular conformational epitope of P-glycoprotein
Suitable for ELISA, Inhib, FuncS
Isotype: IgG
Clonality: Monoclonal
Various conjugated forms available upon request.
Summary
Specifications
Antibody Isotype
IgG
Clone
UIC2
Species Reactivity
Human
Immunogen
Mouse Balb/c 3T3 fibroblasts transfected with human CD243 cDNA.
Conjugate
Unconjugated
Applications
Application Notes
ELISA, Inhib, FuncS Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.
General Notes
ABCB1 (also termed P-glycoprotein) is a physiologically essential multidrug efflux transporter of key relevance to biomedicine. Clone UIC2 targets the extracellular moiety of human ABCB1 and has been successfully used to investigate the transport cycle of ABCB1 owing to its ability to bind the transporter during various states of the catalytic cycle.
Target
Alternative Names
ABCB1; ATP-binding cassette, sub-family B (MDR/TAP), member 1; CLCS; MDR1; P-GP; PGY1; ABC20; CD243; GP170; multidrug resistance protein 1; P-glycoprotein 1; colchicin sensitivity; doxorubicin resistance;
Citations
Publication ()
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References
Structural insight into substrate and inhibitor discrimination by human P-glycoprotein.
ABCB1, also known as P-glycoprotein, actively extrudes xenobiotic compounds across the plasma membrane of diverse cells, which contributes to cellular drug resistance and interferes with therapeutic drug delivery. We determined the 3.5-angstrom cryo-electron microscopy structure of substrate-bound human ABCB1 reconstituted in lipidic nanodiscs, revealing a single molecule of the chemotherapeutic compound paclitaxel (Taxol) bound in a central, occluded pocket. A second structure of inhibited, human-mouse chimeric ABCB1 revealed two molecules of zosuquidar occupying the same drug-binding pocket. Minor structural differences between substrate- and inhibitor-bound ABCB1 sites are amplified toward the nucleotide-binding domains (NBDs), revealing how the plasticity of the drug-binding site controls the dynamics of the adenosine triphosphate-hydrolyzing NBDs. Ordered cholesterol and phospholipid molecules suggest how the membrane modulates the conformational changes associated with drug binding and transport.
COA
Publication 
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