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

Name: Rabbit Anti-DROSHA Recombinant Antibody (D28B1)
SKU: CBMAB-D1697-YC
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Rabbit

Clone

D28B1

Application

WB, IP

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.

More Infomation

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

Human	29102
Mouse	14000

UniProt ID

Human	Q9NRR4
Mouse	Q5HZJ0

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

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

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