| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Death domain-associated protein 6;Daxx;hDaxx;ETS1-associated protein 1;EAP1;Fas death domain-associated protein;DAXX;BING2, DAP6; |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Form | Liquid |
| Host | |
| Immunogen | A synthesized peptide derived from human RUNX2. |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Storage | |
| Target | |
| UniProt # |
Overview
This product is an anti-RUNX2 antibody for target detection and characterization. Key identifiers include host species: Rabbit; Monoclonal; clone HCO-18; isotype Rabbit IgG; reactivity: Human,Mouse,Rat. Reported application contexts include IF, IHC, ICC, WB (as provided in the source record). Boster Bio Anti-RUNX2 Monoclonal Antibody catalog # M00442. Tested in WB, IHC, ICC/IF applications. This antibody reacts with Human, Mouse, Rat.
Key elements and design rationale
- Target: RUNX2 (Death domain-associated protein 6).
- Antibody format: Monoclonal; clone HCO-18; isotype Rabbit IgG.
- Host: Rabbit.
- Species reactivity: Human,Mouse,Rat (confirm in your model system with appropriate controls).
This description is intended to help interpret the antibody design and the biological context of the target using the fields provided in the catalog record, alongside general experimental considerations.
Biological background
RUNX2 (protein: T-cell surface glycoprotein CD4) is a commonly studied target in molecular and cellular biology. Functional context (as provided): Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activatiopn of PAX3 and ETS1 through protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upopn neuronal activation asociates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML- NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). . Reported cellular localization context: Cytoplasm. Nucleus, nucleoplasm. Nucleus, PML body . Nucleus, nucleolus. Chromosome, centromere. Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures. Tissue expression notes (as provided): Ubiquitous.
Research relevance and current trends
- Research context keywords from the source record include: Cancer,Chromatin Binding Proteins,Developmental Biology,DNA/RNA Binding,Epigenetics and Nuclear Signaling,Hematopoietic Progenitors,Mesenchymal Stem Cells,Neurogenesis,Neurology Process,Neuroscience,Oncoproteins,Oncoproteins/Suppressors,Organogenesis,Skeletal Development,Stem Cells,Transcription,Transcription Factors.
- Current studies often focus on connecting target abundance/localization to pathway perturbations across models, tissues, and cell states.
- Quantitative and multiplexed assays (e.g., imaging + immunoblot panels) are commonly used to compare phenotypes across conditions and time-courses.
Common research applications
- Western blotting (WB): assess relative target abundance across samples, treatments, or time-points.
- Immunohistochemistry (IHC): evaluate spatial distribution of target-positive staining in tissue architecture.
- Immunofluorescence/ICC (IF/ICC): visualize subcellular localization patterns and cell-to-cell heterogeneity.
Workflow ideas (metafield): Validate RUNX2 antibody specificity using KO/KD control samples (WB/IF/IHC as appropriate), Detect RUNX2 expression by Western blot in cell or tissue lysates, Detect RUNX2 in FFPE tissue sections by immunohistochemistry, Localize RUNX2 by immunofluorescence/immunocytochemistry in cultured cells
Notes for experimental interpretation
- Consider isoforms and post-translational modifications (PTMs) that may shift apparent molecular weight or epitope accessibility.
- Apparent molecular weight may vary by sample type and processing (observed MW: 57 kDa).
- Control concepts: include appropriate negative controls (e.g., isotype, KO/KD samples) and orthogonal validation when feasible.
Additional product details (from the source record)
- Molecular weight (observed): 57 kDa
- Cellular localization (provided): Cytoplasm. Nucleus, nucleoplasm. Nucleus, PML body . Nucleus, nucleolus. Chromosome, centromere. Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures.
- Tissue details (provided): Ubiquitous.
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.
