HO-1 Antibody - #AF5393

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Product: HO-1 Antibody
Catalog: AF5393
Description: Rabbit polyclonal antibody to HO-1
Application: WB IHC
Cited expt.: WB, IHC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 33 kDa; 33kD(Calculated).
Uniprot: P09601
RRID: AB_2837878

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MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user. For optimal experimental results, antibody reuse is not recommended.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Polyclonal
Specificity:
HO-1 Antibody detects endogenous levels of total HO-1.
RRID:
AB_2837878
Cite Format: Affinity Biosciences Cat# AF5393, RRID:AB_2837878.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

32 kD; bK286B10; D8Wsu38e; heat shock protein 32 kD; heat shock protein 32kD; Heat shock protein; Heme oxygenase (decycling) 1; Heme oxygenase 1; Hemox; HMOX 1; Hmox; Hmox1; HMOX1_HUMAN; HO 1; HO; HO-1; HO1; Hsp32;

Immunogens

Immunogen:

A synthesized peptide derived from human HO-1, corresponding to a region within the internal amino acids.

Uniprot:

P09601(HMOX1_HUMAN) >>Visit HPA database.

Gene(ID):
HMOX1(3162)
Expression:
P09601 HMOX1_HUMAN:

Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level).

Description:
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.
Sequence:
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM

Research Backgrounds

Function:

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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

Subcellular Location:

Microsome. Endoplasmic reticulum membrane>Peripheral membrane protein>Cytoplasmic side.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level).

Family&Domains:

Belongs to the heme oxygenase family.

Research Fields

· Cellular Processes > Cell growth and death > Ferroptosis.   (View pathway)

· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway.   (View pathway)

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > MicroRNAs in cancer.

· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.   (View pathway)

· Metabolism > Metabolism of cofactors and vitamins > Porphyrin and chlorophyll metabolism.

· Metabolism > Global and overview maps > Metabolic pathways.

· Organismal Systems > Digestive system > Mineral absorption.

References

1). Ultrasmall PtAu2 nanoclusters activate endogenous anti-inflammatory and anti-oxidative systems to prevent inflammatory osteolysis. Theranostics, 2023 (PubMed: 36793859) [IF=12.4]
2). Mitochondria-targeted supramolecular coordination container encapsulated with exogenous itaconate for synergistic therapy of joint inflammation. Theranostics, 2023 (PubMed: 35547753) [IF=12.4]
3). Repurposing melatonin's therapeutic potential in Wilson disease: Addressing copper overload and redox imbalance. Redox biology, 2026 (PubMed: 41406573) [IF=10.7]

Application: WB    Species: human    Sample: HepG2cells

Figure 5. Melatonin Restores Redox Balance by Modulating Nrf2–HO-1 Signalling and Glutathione Oxidation (A) Representative immunofluorescence images showing Nrf2 localization in ATP7B⁻ /⁻_HepG2 cells under basal, copper-treated,copper + melatonin, copper +D-Pen and copper+NAC conditions. Nuclei were counterstained with DAPI (blue); Nrf2 is shown in Red. Scale bar: 10 μM. (B) Quantification of nuclear Nrf2 localization in ATP7B⁻ /⁻_HepG2 cells reveal increased nuclear Nrf2 translocation upon copper exposure (~91.76% in KO), which was significantly reduced by melatonin pretreatment (~20.36% in KO). Nrf2 nuclear localization also decreases after NAC treatment (29.2%) and D-Pen (30.78%) which is lesser than melatonin. (C) Western blot showing HO-1 expression in WT_HepG2 and ATP7B⁻ /⁻_HepG2 cells under the indicated treatments. (D) Densitometric quantification of HO-1 band intensity normalized to α-tubulin. Copper exposure induces HO-1 expression, which is markedly reduced upon melatonin treatment. These results demonstrate that melatonin dampens copper-induced oxidative stress by inhibiting nuclear translocation of Nrf2 and downregulating its downstream target HO-1, thereby restoring redox homeostasis in both WT_HepG2 and 456 ATP7B⁻ /⁻_HepG2 cells. (E) Pseudocolor ratiometric images of GRX1-roGFP2 are shown for WT_HepG2 and ATP7B⁻ /⁻_HepG2 cells (top panel), along with ATP7B-/- _HepG2 cells treated with melatonin for 2 hours and 18 hours, respectively (bottom panel). The images were acquired under live-cell conditions using a 63X oil immersion lens. Scale bar: 20 μM. (F) Relative mean fluorescence intensity of the 405/488 ratio for GRX1- roGFP2 shows the following mean values: WT_HepG2 cells (0.5469), ATP7B-/-_HepG2 cells (0.7208), ATP7B-/-_HepG2 cells + MLT for 2 hours (0.5093), and ATP7B (-/-) + MLT for 18 hours (0.4541). α-tubulin was used as a loading control for all immunoblot analyses. Data represent mean ± SD from three or more independent experiments. Statistical analysis was performed using an unpaired t-test. *p < 0.05; **p < 0.01; **p < 0.001.
4). Near-infrared organic nanoparticles (6BQ NPs) enhance the random flaps survival by modulating the HSP90/HIF-1α axis through mild photothermal therapy. Journal of nanobiotechnology, 2025 (PubMed: 40652210) [IF=10.2]

Application: WB    Species: human    Sample: HUVECs

Fig. 3. 6BQ NPs promote angiogenesis in vitro by modulating the HSP90/HIF-1α axis through MPTT, while inhibiting oxidative stress and inflammatory responses. A, B, C mRNA expression of HIF-1α, HSP90 and VEGF in HUVECs of every group was measured by RT-qPCR. D Western blotting of HIF-1α, HSP90 and VEGF expressions in HUVECs of the three groups. E Western blotting of HO-1 and SOD1 expressions in HUVECs of the three groups. F Western blotting of IL-6 expressions in HUVECs of the three groups. G The optical density values of HIF-1α, HSP90 and VEGF in HUVECs of the three groups. H The optical density values of HO-1 and SOD1 in HUVECs of the three groups. I The optical density values of IL-6 in HUVECs of the three groups. J Mean SOD activity of HUVECs in the three groups. K Mean MDA content of HUVECs in the three groups. Data are presented as mean ± SD, n = 6 per group. ns P > 0.05, **P 
5). Curcumin-loaded milk-derived sEVs fused with platelet membrane attenuate endothelial senescence and promote spinal cord injury recovery in diabetic mice. Materials today. Bio, 2025 (PubMed: 40688662) [IF=8.7]

Application: WB    Species: human    Sample:

Fig. 3. Reduction in HG/IL-1β-induced senescence markers and TJ protein degradation in HUVECs by Cur treatment. (A) Typical images of HUVECs stained with SA-β-gal (blue stain indicates senescent cells). The number of SA-β-gal+ cells decreased in the Cur group compared to the HG/IL-1β + DMSO group, whereas it increased after brusatol treatment. Scale bar = 200 μm. (B) Quantification of SA-β-gal+ cells (n = 5). (C) Typical images of Claudin-5 staining (green, TJ protein). The intensity of Claudin-5 increased in the Cur group compared to the HG/IL-1β + DMSO group, which was decreased by brusatol treatment. Scale bar = 100 μm. (D) Quantification of the relative fluorescence intensity of Claudin-5 (n = 5). (E) Analysis of VE-Cadherin, ZO-1, Occludin and Claudin-5 expression in HUVECs by WB (TJ protein). The level of TJ protein was increased in the Cur group compared to the HG/IL-1β + DMSO group, which was decreased by brusatol treatment. (F–I) Quantification of the level of VE-Cadherin, ZO-1, Claudin-5, Occludin (n = 3). (J) Analysis of NRF2, HO-1, P21 and P16 expression in HUVECs by WB. Note: (1) The levels of NRF2 and HO-1 were upregulated in the Cur group compared to the HG/IL-1β + DMSO group, which was reduced by brusatol treatment. (2) The levels of P21 and P16 were decreased in the Cur group compared to the HG/IL-1β + DMSO group, which were increased by brusatol treatment. (K–N) Quantification of NRF2, HO-1, P21, and P16 levels (n = 3). ∗P < 0.05, ∗∗P < 0.01. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
6). Cytotoxicity of adducts formed between quercetin and methylglyoxal in PC-12 cells. Food Chemistry, 2021 (PubMed: 33706136) [IF=8.5]

Application: WB    Species: Rat    Sample: PC-12 cells

Fig. 5. Effect of treatments of MGO, Que-mono-MGO, and Que-di-MGO on the expression levels of apoptotic markers and components of AKT and Nrf2-HO-1/NQO-1 signaling pathways. Significant differences (p < 0.05) between samples of different treatments are marked with different letters on each column.
7). Targeted Reprogramming of Macrophages by Nanozyme for Accelerated Wound Healing. ACS applied materials & interfaces, 2025 (PubMed: 40521762) [IF=8.3]
8). Amelioration of arsenic-induced hepatic injury via sulfated glycosaminoglycan from swim bladder: Modulation of Nrf2 pathway and amino acid metabolism. International journal of biological macromolecules, 2024 (PubMed: 39653196) [IF=8.2]
9). Cetuximab promotes RSL3-induced ferroptosis by suppressing the Nrf2/HO-1 signalling pathway in KRAS mutant colorectal cancer. Cell Death & Disease, 2021 (PubMed: 34775496) [IF=8.1]

Application: WB    Species: Human    Sample: HCT116 and DLD-1 cells

Fig. 3 Combination treatment with RSL3 and cetuximab inhibits Nrf2/HO-1 axis in KRAS mutant CRC cells. A The protein levels of Keap1, Nrf2 and HO-1 in HCT116 and DLD-1 cells were measured by western blotting after treatment with RSL3 (1 μM), cetuximab (100 μg/ml) or their combination for 24 h. B Knockdown of Nrf2 by siRNA reduced the expression of Nrf2 and the protein levels of Nrf2 and HO-1 after treatment with RSL3 (1 μM) for 24 h. C siRNA-mediated knockdown of Nrf2 increased the sensitivity of HCT116 and DLD-1 cells to RSL3. D–F The levels of MDA, lipid ROS and intracellular iron were measured in Nrf2-silenced HCT116 and DLD-1 cells pretreated with or without RSL3 (1 μM). Scale bar, 100 μm. **P < 0.01; *P < 0.05.
10). Structural features of polysaccharides from Physalis pubescens L. stem, and their neuroprotective effects and anti-aging activities. International journal of biological macromolecules, 2025 (PubMed: 40975332) [IF=7.7]
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