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Rabbit Anti-DROSHA Recombinant Antibody (D28B1) (CBMAB-D1697-YC)

Provided herein is a Rabbit monoclonal antibody, which binds to Drosha Ribonuclease III (DROSHA). The antibody can be used for immunoassay techniques, such as WB, IP.
See all DROSHA antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse
Clone
D28B1
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Specificity
Human, Mouse
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
Drosha Ribonuclease III
Introduction
DROSHA is a ribonuclease (RNase) III double-stranded RNA-specific ribonuclease and subunit of the microprocessor protein complex, which catalyzes the initial processing step of microRNA (miRNA) synthesis. The encoded protein cleaves the stem loop structure from the primary microRNA (pri-miRNA) in the nucleus, yielding the precursor miRNA (pre-miRNA), which is then exported to the cytoplasm for further processing. In a human cell line lacking a functional copy of this gene, canonical miRNA synthesis is reduced. Somatic mutations in this gene have been observed in human patients with kidney cancer.
Entrez Gene ID
Human29102
Mouse14000
UniProt ID
HumanQ9NRR4
MouseQ5HZJ0
Alternative Names
Drosha Ribonuclease III; Drosha, Double-Stranded RNA-Specific Endoribonuclease; Ribonuclease Type III, Nuclear; Drosha, Ribonuclease Type III; EC 3.1.26.3; RNase III; RNASE3L; RNASEN; P241; RN3;
Research Area
Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease 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, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. Involved also in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in the formation of GW bodies.
Biological Process
Defense response to Gram-negative bacterium Source: UniProtKB
Defense response to Gram-positive bacterium Source: UniProtKB
miRNA metabolic process Source: Ensembl
Positive regulation of gene expression Source: Ensembl
Pre-miRNA processing Source: GO_Central
Primary miRNA processing Source: WormBase
Production of siRNA involved in RNA interference Source: GO_Central
Regulation of inflammatory response Source: Ensembl
Regulation of miRNA metabolic process Source: Ensembl
Regulation of regulatory T cell differentiation Source: Ensembl
Ribosome biogenesis Source: UniProtKB-KW
RNA processing Source: GO_Central
rRNA catabolic process Source: InterPro
Cellular Location
Nucleus; Nucleolus. A fraction is translocated to the nucleolus during the S phase of the cell cycle. Localized in GW bodies (GWBs), also known as P-bodies.

Xu, H., Liu, X., Li, W., Xi, Y., Su, P., Meng, B., ... & Mao, Z. (2021). p38 MAPK‐mediated loss of nuclear RNase III enzyme Drosha underlies amyloid beta‐induced neuronal stress in Alzheimer's disease. Aging cell, 20(10), e13434.

Hajirostamlou, M., & Ghorbian, S. (2021). Evaluation of the clinical significance of RNase III enzyme DROSHA in pediatrics acute lymphocytic leukemia. Molecular Biology Reports, 48(1), 451-456.

Peng, F., Xu, J., Cui, B., Liang, Q., Zeng, S., He, B., ... & Liu, Q. (2021). Oncogenic AURKA-enhanced N6-methyladenosine modification increases DROSHA mRNA stability to transactivate STC1 in breast cancer stem-like cells. Cell research, 31(3), 345-361.

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.

Cho, S. J., Hong, K. S., Jeong, J. H., Lee, M., Choi, A. M., Stout-Delgado, H. W., & Moon, J. S. (2019). DROSHA-dependent AIM2 inflammasome activation contributes to lung inflammation during idiopathic pulmonary fibrosis. Cells, 8(8), 938.

Pong, S. K., & Gullerova, M. (2018). Noncanonical functions of micro RNA pathway enzymes–Drosha, DGCR 8, Dicer and Ago proteins. FEBS letters, 592(17), 2973-2986.

Kim, K., Nguyen, T. D., Li, S., & Nguyen, T. A. (2018). SRSF3 recruits DROSHA to the basal junction of primary microRNAs. Rna, 24(7), 892-898.

Kim, S., Song, M. L., Min, H., Hwang, I., Baek, S. K., Kwon, T. K., & Park, J. W. (2017). miRNA biogenesis‑associated RNase III nucleases Drosha and Dicer are upregulated in colorectal adenocarcinoma. Oncology Letters, 14(4), 4379-4383.

Kim, B., Jeong, K., & Kim, V. N. (2017). Genome-wide mapping of DROSHA cleavage sites on primary microRNAs and noncanonical substrates. Molecular cell, 66(2), 258-269.

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

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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