Monoclonal Anti-DICER1 antibody produced in mouse

Dicer is a member of the RNase III family containing an N-terminal DEXH-box RNA helicase/ATPase domain, followed by a domain of unknown function (DUF283), a PAZ domain, which anchors the 3′-end of the guided siRNA, two RNase III domains, and a dsRBD. The current model for dsRNA cleavage by Dicer predicts that the two ribonuclease III domains of Dicer dimerize to form the catalytic center that is responsible for cleaving long dsRNA in co-operation with two RNA binding domains, PAZ and dsRNA-binding domain.

Monoclonal Anti-DICER1 (mouse IgG1 isotype) is derived from the hybridoma DCR1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a fusion protein corresponding to a fragment of human DICER1.

The antibody may be used in several immunological techniques including immunoblotting and real‐time PCR.

Dicer catalyzes the first step in the RNA interference (RNAi) pathway and initiates formation of the RNA-induced silencing complex (RISC). The dsRNA is processed into small fragments called short interfering RNA (siRNA) or microRNA (miRNA) of typically 21-25 nucleotides long with a two-base overhang on the 3′ end. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. DICER1-deficient colorectal cancer cells have an enhanced ability to initiate tumors and metastasis. Dicer functions as an indirect tumor suppressor, as silencing Dicer expression makes cancer cells more malignant.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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