| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | ATP synthase F (0) complex subunit C1,2,3, mitochondrial; ATP synthase lipid-binding protein; ATP synthase membrane subunit c locus 1,2,3; ATP synthase proteolipid P1; ATP synthase proton-transporting mitochondrial F (0) complex subunit C1,2,3; ATPase protein 9; ATPase subunit c; ATP5MC1,2,3; ATP5G1,2,3 |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E.coli-derived human RIOK2 recombinant protein (Position: D16-L283). |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-RIOK2 Antibody Picoband® is an antibody reagent for detection of RIOK2 (ATP synthase membrane subunit c locus 1,2,3). Researchers commonly use anti-RIOK2 antibodies to measure relative expression and localization across biological samples, with assay selection guided by the listed applications (WB, IHC, Flow, ELISA).
Boster Bio Anti-RIOK2 Antibody Picoband® catalog # A09743-1. Tested in ELISA, Flow Cytometry, WB applications. This antibody reacts with Human. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.
Key elements and design rationale
- Target: RIOK2 (ATP synthase membrane subunit c locus 1,2,3). Alternative names: ATP synthase F (0) complex subunit C1,2,3, mitochondrial; ATP synthase lipid-binding protein; ATP synthase membrane subunit c locus 1,2,3; ATP synthase proteolipid P1; ATP synthase proton-transporting mitochondrial F (0) complex subunit C1,2,3; ATPase protein 9; ATPase subunit c; ATP5MC1,2,3; ATP5G1,2,3
- Antibody format: Polyclonal; Rabbit IgG
- Species context: Host: Rabbit, Reactivity: Human
- Purification: Immunogen affinity purified.
- Immunogen: E.coli-derived human RIOK2 recombinant protein (Position: D16-L283).
- Molecular weight context: observed 63 kDa, calculated 67169 MW (reported)
- Provided application(s): WB, IHC, Flow, ELISA
These attributes help contextualize how the antibody is commonly selected (host/clonality/isotype/label) and how signals are interpreted across sample types and assay formats.
Biological background
Function: Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Cellular localization: Mitochondrion membrane. Multi-pass membrane protein.
Tissue details: Highly expressed in thymus, uterus and testis. Detected at lower levels in brain, mammary gland, prostate, salivary gland and fetal spleen. In brain, highest expression in thalamus, hippocampus and amygdala. .
Background: RIO kinase 2 (RIOK2) is a member of the RIO family of atypical serine protein kinases first characterized in yeast. There are three RIO kinase subfamilies: RIO1, RIO2, and RIO3. RIOK1 and RIOK2 proteins are present in organisms from Archaea to humans. Studies of RIO kinases in yeast indicate that they play a role in ribosome biogenesis. Human RIOK2 has been shown to be a part of a late 40S pre-ribosomal particle and have influence on 40S maturation.
Cross reactivity: No cross-reactivity with other proteins.
Research relevance and current trends
- Quantitative and spatial profiling: expression patterns are increasingly studied across cell states using multiplex imaging and omics-informed validation.
- Isoforms and post-translational modifications: researchers often evaluate how isoform composition and PTMs can shift apparent molecular weight or localization.
- Context-aware interpretation: comparative studies commonly include perturbations (stimulation, inhibition, genetic models) to relate target changes to pathway behavior.
Common research applications
- Western blot (WB): compare relative target abundance and apparent size shifts (e.g., isoforms/PTMs) across conditions.
- Immunohistochemistry (IHC): assess distribution across tissue compartments and compare staining patterns between groups.
- Flow cytometry: quantify target-positive populations and compare shifts after stimulation or differentiation.
Across these uses, researchers typically interpret changes in signal as relative differences between matched sample groups, considering sample preparation and biological context.
Notes for experimental interpretation
- Apparent molecular weight can vary due to isoforms, proteolysis, glycosylation, phosphorylation, and sample preparation differences.
- Species reactivity and epitope conservation can influence observed signal patterns, especially in cross-species studies.
- Control concepts: include appropriate negative controls (e.g., isotype controls where relevant) and, when feasible, genetic or orthogonal controls (KO/KD, peptide competition, or independent assays) to support interpretation.
For antibody reagents, monoclonal antibodies are often chosen for epitope consistency across lots, while polyclonals may recognize multiple epitopes and can show different background characteristics depending on context.
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.