The peptide is totally conserved in pig, rat and mouse HO-1; three amino acid substitutions (A16L; A20G; V24A) exist in the aligned region (residues 31-44) within human, rat and rabbit HO-2; and a single change (A16L) exists in chicken HO.
Product Details
| Alternative Name: | HMOX1, Hsp32, Heat shock protein 32, HO-1 |
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| Host: | Rabbit |
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| Immunogen: | Synthetic peptide corresponding to aa 12-25 of human heme oxygenase 1 (HO-1) protein. |
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| UniProt ID: | P09601 |
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| Source: | Purified from rabbit serum. |
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| Species reactivity: | Human
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| Applications: | IHC, WB
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| Recommended Dilutions/Conditions: | Immunohistochemistry (1:50-1:1,000)
Western Blot (1:1,000)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application. |
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| Blocking Peptide: | For Blocking peptide see Prod. No. BML-HP9301.
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| Purity Detail: | Protein A affinity purified. |
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| Formulation: | Liquid. In PBS containing 0.09% sodium azide. |
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| Handling: | Store unopened vial at -20°C until required for use. Store diluted antibody at 2-4°C and use within 1 month. Avoid freeze/thaw cycles. |
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| Shipping: | Blue Ice |
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| Long Term Storage: | -20°C |
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| Scientific Background: | The rate limiting enzyme in heme catabolism, heme oxygenase, was first described in 1968 and was thought to be a species of cytochrome P450. However, subsequent work showed the enzyme to be a protein distinct from the P450 family and capable of catalysing the degradation of heme to biliverdin and iron, with the concomitant release of carbon monoxide. This enzyme activity is highly conserved throughout the Animal Kingdom and has been identified in algae and plants as well as in all higher species. Heme oxygenase-1 (HO-1) was first purified to homogeneity from rat liver and pig spleen and shown to have a molecular weight of 32kDa. Increased expression of HO-1 can be induced by a large number of structurally unrelated pharmacological and other agents, including cytokines and oxidants, as well as by heat shock and other forms of cellular stress. Baseline levels of HO-1 expression are high in certain tissues, including spleen and liver, but enriched enzyme preparations are recommended for experimental analysis. Recent data have demonstrated a cytoprotective role for HO-1, preventing cell death by modulating intracellular iron levels. |
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| Regulatory Status: | RUO - Research Use Only |
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Western blot analysis: HO-1 was detected using HO-1, pAb (Prod. no. BML-HC3001) (lanes 1, 3, 5 and 7), and HO-2 was detected using HO-2, pAb (Prod. no. BML-HC3002) (lanes 2, 4, 6 and 8). Both antibodies were used at a dilution of 1:1000. Luminograph (ECL, 15 sec. exposure, ref. FM020/054) showing HO-1 and HO-2 expression in lysates prepared from gIFN/LPS stimulated RAW264.7 mouse macrophage cells (lanes 1 and 2), HepG2 (lanes 3 and 4), rat testis (HP9312, lanes 5 and 6) and rat spleen (HP9313, lanes 7 and 8).
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Product Literature References
Heme oxygenase-2 (HO-2) binds and buffers labile ferric heme in human embryonic kidney cells: D.A. Hanna, et al.; J. Biol. Chem.
298, 101549 (2022),
Abstract;
TLR4 Signaling and Heme Oxygenase-1/Carbon Monoxide Pathway Crosstalk Induces Resiliency of Myeloma Plasma Cells to Bortezomib Treatment: G. Scandura, et al.; Antioxidants
11, 767 (2022),
Abstract;
Esomeprazole attenuates inflammatory and fibrotic response in lung cells through the MAPK/Nrf2/HO1 pathway: A. Ebrahimpour, et al.; J. Inflamm.
18, 12950 (2021),
Abstract;
Full Text
Characterization of cadmium chloride-induced BiP accumulation in Xenopus laevis A6 kidney epithelial cells: C.S. Shirriff, et al.; Comp. Biochem. Physiol. C. Toxicol. Pharmacol.
191, 117 (2016),
Application(s): Protein isolation and immunoblot analysis, A6 cells,
Abstract;
Chemical characterization, free radical scavenging, cellular antioxidant and anti-inflammatory properties of a stilbenoid-rich root extract of Vitis vinifera: T. Esatbeyoglu, et al.; Oxid. Med. Cell. Longev.
2016, Article ID 8591286 (2016),
Application(s): Western Blot,
Abstract;
Full Text
Hormonal fluctuations during the estrous cycle modulate heme oxygenase-1 expression in the uterus: M.L. Zenclussen, et al.; Front. Endocrinol. (Lausanne)
5, 32 (2014),
Application(s): WB using cell lysates of human uterine cell line (AN3),
Abstract;
Full Text
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