| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Transcription factor Sp1; SP1; TSFP1 |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E.coli-derived human DROSHA recombinant protein (Position: H1142-K1374). |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-DROSHA Antibody Picoband® is an antibody for DROSHA detection raised in Rabbit (Polyclonal, Rabbit IgG), with reported reactivity: Human,Mouse,Rat. Commonly used in WB, IHC, IF, ICC, Flow Cytometry, ELISA workflows.
Key elements and design rationale
- Target: DROSHA (transcription factor); UniProt: Q9NRR4
- Antibody format: Rabbit, Polyclonal, Rabbit IgG
- Molecular weight: 159 kDa, calculated 33275 MW
- Applications: WB, IHC, IF, ICC, Flow Cytometry, ELISA
Vendor description (summary): Boster Bio Anti-DROSHA Antibody Picoband® catalog # A00111-4.
Biological background
Biological context: Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR- alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component ARNTL/BMAL1.
Expression and localization notes: cellular localization: Nucleus. Cytoplasm. Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location., tissue context: Up-regulated in adenocarcinomas of the stomach (at protein level). Isoform 3 is ubiquitously expressed at low levels..
Common research applications
- Western blotting (WB): Compare DROSHA levels across samples and conditions using appropriate loading and biological controls.
- Immunohistochemistry (IHC): Evaluate spatial distribution of DROSHA in tissue sections, considering fixation and antigen retrieval effects.
- Immunofluorescence / ICC: Assess subcellular localization patterns and co-localization with compartment markers in cultured cells.
- Flow cytometry: Quantify DROSHA-positive populations in single-cell suspensions with appropriate gating and controls.
- ELISA: Use antibody-based detection formats to assess antigen presence or binding in plate-based assays.
Notes for experimental interpretation
- Account for isoforms, post-translational modifications, and sample-specific processing that can shift apparent molecular weight or epitope accessibility.
- Use positive/negative biological controls where possible (e.g., known-expressing cells/tissues, knockdown/knockout models) and include appropriate secondary-only/isotype controls for imaging workflows.
Additional product notes (from provided fields)
- Background: Drosha is a Class 2 ribonuclease III enzyme that in humans is encoded by the DROSHA (formerly RNASEN) gene. This gene encodes 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.
- Cross reactivity: No cross-reactivity with other proteins.
- Cellular localization: Nucleus. Cytoplasm. Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location.
- Tissue details: Up-regulated in adenocarcinomas of the stomach (at protein level). Isoform 3 is ubiquitously expressed at low levels.
- Research category: 2339,Domain Families,Epigenetics and Nuclear Signaling,Metabolic Signaling Pathways,Metabolism,Mitochondrial Metabolism,Nuclear,Nucleotide Metabolism,Pathways and Processes,Signaling Pathways,Stem Cells,TGF Beta,Transcription,Zinc Finger
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
