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Rabbit Anti-DROSHA Recombinant Antibody (D1698) (V2LY-0425-LY942)

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Summary

Host Animal
Rabbit
Specificity
Human, Mouse
Clone
D1698
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Immunogen
Synthetic peptide corresponding to residues surrounding Gly953 of human Drosha.
Host Species
Rabbit
Specificity
Human, Mouse
Antibody Isotype
IgG
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:1,000
IP1:50

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

Format
Liquid
Buffer
BSA & Glycerol & HEPES
Preservative
Sodium Azide
Concentration
Batch dependent
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.

Custom Antibody Labeling

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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