Product nameAnti-DGCR8 antibody - N-terminal
See all DGCR8 primary antibodies
DescriptionRabbit polyclonal to DGCR8 - N-terminal
Tested applicationsSuitable for: WB, IPmore details
Species reactivityReacts with: Human
Predicted to work with: Rhesus monkey
Recombinant fragment within Human DGCR8 (N terminal). The exact sequence is proprietary.
Database link: Q8WYQ5
- WB: HEK-293T, A431, HeLa and HepG2 whole cell extracts. IP: Jurkat whole cell extract.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferpH: 7.00
Preservative: 0.025% Proclin
Constituents: PBS, 20% Glycerol
Concentration information loading...
PurityImmunogen affinity purified
- HeLa whole cell lysate (ab150035)
- HepG2 whole cell lysate (ab166833)
- HeLa whole cell lysate (ab29545)
- Jurkat whole cell lysate (ab30128)
- A431 whole cell lysate (ab30132)
- Jurkat whole cell lysate (ab7899)
- HepG2 whole cell lysate (ab7900)
- A431 whole cell lysate (ab7909)
- 293T whole cell lysate (ab95494)
Our Abpromise guarantee covers the use of ab227581 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/500 - 1/3000. Predicted molecular weight: 86 kDa.|
|IP||1/100 - 1/500.|
FunctionComponent of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri-miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri-miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding. Involved in the silencing of embryonic stem cells self-renewal.
Tissue specificityUbiquitously expressed.
Sequence similaritiesContains 2 DRBM (double-stranded RNA-binding) domains.
Contains 1 WW domain.
DomainBoth DRBM domains are required for efficient binding to pri-miRNA. The region between residues 276 and 498 has an autoinhibitory function on pri-miRNA processing activity.
Cellular localizationNucleus. Nucleus > nucleolus. Colocalizes with nucleolin and DROSHA in the nucleolus. Mostly detected in the nucleolus as electron-dense granular patches around the fibrillar center (FC) and granular component (GC). Also detected in the nucleoplasm as small foci adjacent to splicing speckles near the chromatin structure. Localized with DROSHA in GW bodies (GWBs), also known as P-bodies.
- Information by UniProt
- DGCRK6 antibody
- C22orf12 antibody
- D16H22S788E antibody
All lanes : Anti-DGCR8 antibody - N-terminal (ab227581) at 1/1000 dilution
Lane 1 : HEK-293T (human epithelial cell line from embryonic kidney transformed with large T antigen) whole cell extract
Lane 2 : A431 (human epidermoid carcinoma cell line) whole cell extract
Lane 3 : HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell extract
Lane 4 : HepG2 (human liver hepatocellular carcinoma cell line) whole cell extract
Lysates/proteins at 30 µg per lane.
Predicted band size: 86 kDa
7.5% SDS-PAGE gel.
DGCR8 was immunoprecipitated from Jurkat (human T cell leukemia cell line from peripheral blood) whole cell extract with 5 μg ab227581. Western blot was performed from the immunoprecipitate using ab227581.
Lane 1: Control IgG instead of ab227581 in Jurkat whole cell extract.
Lane 2: ab227581 IP in Jurkat whole cell extract.
ab227581 has not yet been referenced specifically in any publications.