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Mouse Anti-DROSHA Recombinant Antibody (D1697) (V2LY-0425-LY941)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
D1697
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 1071-1370 mapping at the C-terminus of human RNase III.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
ELISA1:100-1:1,000
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500

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

Format
Liquid
Buffer
Gelatin & PBS
Preservative
Sodium Azide
Concentration
0.2 mg/ml
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Drosha Ribonuclease III
Entrez Gene ID
Human29102
Mouse14000
UniProt ID
HumanQ9NRR4
MouseQ5HZJ0
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.
More Infomation

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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