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Mouse Anti-DGCR8 Recombinant Antibody (E-10) (CBMAB-D0765-YC)

Provided herein is a Mouse monoclonal antibody, which binds to DGCR8, Microprocessor Complex Subunit (DGCR8). The antibody can be used for immunoassay techniques, such as WB, IP, IF, ELISA.
See all DGCR8 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
E-10
Antibody Isotype
IgG
Application
WB, IP, IF, ELISA

Basic Information

Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
DGCR8, Microprocessor Complex Subunit
Introduction
DGCR8 is a subunit of the microprocessor complex which mediates the biogenesis of microRNAs from the primary microRNA transcript. The encoded protein is a double-stranded RNA binding protein that functions as the non-catalytic subunit of the microprocessor complex. This protein is required for binding the double-stranded RNA substrate and facilitates cleavage of the RNA by the ribonuclease III protein, Drosha.
Entrez Gene ID
Human54487
Mouse94223
Rat287954
UniProt ID
HumanQ8WYQ5
MouseQ9EQM6
RatD4A2G4
Alternative Names
DGCR8, Microprocessor Complex Subunit; DiGeorge Syndrome Critical Region Gene 8; DiGeorge Syndrome Critical Region 8; C22orf12; DGCRK6; Microprocessor Complex Subunit DGCR8; Chromosome 22 Open Reading Frame 12; Pasha; Gy1;
Function
Component 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 (PubMed:26027739, PubMed:26748718).

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 (PubMed:15531877, PubMed:15574589, PubMed:15589161, PubMed:16751099, PubMed:16906129, PubMed:16963499, PubMed:17159994).

Specifically recognizes and binds N6-methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing (PubMed:25799998).

Involved in the silencing of embryonic stem cell self-renewal (By similarity).
Biological Process
miRNA metabolic process Source: Reactome
Primary miRNA processing Source: BHF-UCL
Cellular Location
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 (PubMed:17159994).

Paulsson, J. O., Rafati, N., DiLorenzo, S., Chen, Y., Haglund, F., Zedenius, J., & Juhlin, C. C. (2021). Whole-genome sequencing of follicular thyroid carcinomas reveal recurrent mutations in microRNA processing subunit DGCR8. The Journal of Clinical Endocrinology & Metabolism, 106(11), 3265-3282.

Zhao, K., Yang, C., Zhang, J., Sun, W., Zhou, B., Kong, X., & Shi, J. (2021). METTL3 improves cardiomyocyte proliferation upon myocardial infarction via upregulating miR-17-3p in a DGCR8-dependent manner. Cell death discovery, 7(1), 1-14.

Partin, A. C., Zhang, K., Jeong, B. C., Herrell, E., Li, S., Chiu, W., & Nam, Y. (2020). Cryo-EM structures of human Drosha and DGCR8 in complex with primary microRNA. Molecular cell, 78(3), 411-422.

Rivera, B., Nadaf, J., Fahiminiya, S., Apellaniz-Ruiz, M., Saskin, A., Chong, A. S., ... & Foulkes, W. D. (2020). DGCR8 microprocessor defect characterizes familial multinodular goiter with schwannomatosis. The Journal of clinical investigation, 130(3), 1479-1490.

Zhang, F., Ruan, X., Ma, J., Liu, X., Zheng, J., Liu, Y., ... & Xue, Y. (2020). DGCR8/ZFAT-AS1 promotes CDX2 transcription in a PRC2 complex-dependent manner to facilitate the malignant biological behavior of glioma cells. Molecular Therapy, 28(2), 613-630.

Guo, W. T., & Wang, Y. (2019). Dgcr8 knockout approaches to understand microRNA functions in vitro and in vivo. Cellular and Molecular Life Sciences, 76(9), 1697-1711.

Deng, L., Ren, R., Liu, Z., Song, M., Li, J., Wu, Z., ... & Liu, G. H. (2019). Stabilizing heterochromatin by DGCR8 alleviates senescence and osteoarthritis. Nature communications, 10(1), 1-16.

Wen, J., Lv, Z., Ding, H., Fang, X., & Sun, M. (2018). Association of miRNA biosynthesis genes DROSHA and DGCR8 polymorphisms with cancer susceptibility: a systematic review and meta-analysis. Bioscience reports, 38(3).

Partin, A. C., Ngo, T. D., Herrell, E., Jeong, B. C., Hon, G., & Nam, Y. (2017). Heme enables proper positioning of Drosha and DGCR8 on primary microRNAs. Nature communications, 8(1), 1-10.

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For research use only. Not intended for any clinical use.

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