| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Heme oxygenase 2;HO-2;1.14.99.3;HMOX2;HO2; |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E.coli-derived human HMOX2 recombinant protein (Position: S2-M316). Human HMOX2 shares 89% and 90% amino acid (aa) sequences identity with mouse and rat HMOX2, respectively. |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
This antibody is intended for detection of HMOX2 (Heme oxygenase 2) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.
Vendor notes: Boster Bio Anti-Heme oxygenase 2/HMOX2 Antibody Picoband® catalog # PB9213. Tested in IHC, WB applications. This antibody reacts with Human, Mouse, Rat. 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
- Antibody format: Rabbit Polyclonal Rabbit IgG
- Immunogen / epitope context: E.coli-derived human HMOX2 recombinant protein (Position: S2-M316). Human HMOX2 shares 89% and 90% amino acid (aa) sequences identity with mouse and rat HMOX2, respectively. (reported region: S2-M316).
- Molecular weight context: reported MW: 36 kDa; calculated MW: 36 kDa
- Reactivity: Human,Mouse,Rat
- Applications: IHC, WB
As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.
Biological background
Heme oxygenase 2; Heme oxygenase 2. Heme oxygenase 2 (HMOX2), also known as HO-2, is an enzyme that in humans is encoded by the HMOX2 gene. It is mapped to 16p13.3. HMOX2 belongs to the heme oxygenase family. Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. Functional note: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. Reported localization: Microsome. Endoplasmic reticulum.
Research relevance and current trends
- Cancer: Researchers commonly examine how HMOX2 (Heme oxygenase 2) relates to this theme using model systems and orthogonal readouts.
- Cancer Metabolism: Researchers commonly examine how HMOX2 (Heme oxygenase 2) relates to this theme using model systems and orthogonal readouts.
- Metabolism: Researchers commonly examine how HMOX2 (Heme oxygenase 2) relates to this theme using model systems and orthogonal readouts.
Common research applications
- Western blotting: compare relative HMOX2 (Heme oxygenase 2) levels across conditions; band patterns may reflect isoforms and processing.
- IHC/IHC-F: assess spatial distribution of HMOX2 (Heme oxygenase 2) across tissue regions and cell types using matched controls.
Notes for experimental interpretation
- Specificity notes: No cross reactivity with other proteins.
- Cross-reactivity: No cross-reactivity with other proteins
- Family / similarity context: Belongs to the heme oxygenase family.
- Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
- Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.
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.
