Hemoglobin
Based on 4 publication(s) in Google Scholar
Hemoglobin is a iron-containing protein in red blood cells with oxygen binding properties. Hemoglobin is an inducer of HO-1. Hemoglobin consits of heme, which binds to oxygen. Hemoglobin also transports other gases, such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. Hemoglobin absorbs unneeded oxygen in tissues, as an antioxidant.
For research use only. We do not sell to patients.
- CAS No.: 9008-02-0
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Storage:
Please store the product under the recommended conditions in the Certificate of Analysis.
Publications Citing Use of MedChemExpress (MCE) Hemoglobin
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Flow Cytometry
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WB
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Bio/Physico-chemical Assay
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Cell Imaging/Staining
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WB
Biological Activity
Hemoglobin (1-50 μM, 6 h) increases α1-microglobulin and reactive oxygen species in HepG2 cells[3].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
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Animal Model:LPS induced endotoxemia rat model[2]
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Dosage:300 mg/kg
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Administration:i.v., at 16 h before LPS treatment (40 mg/kg, i.v,)
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Result:Increased rat survival.
Showed significant attenuation of neutrophil alveolitis ( > 80 %) at 24 h after LPS injection.
Increased HO-1 expression and activity in rat lung.
| NCT Number | Sponsor | Condition | Start Date |
Phase
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|---|---|---|---|---|
| NCT01329991 | Plexxikon| | 2011-05 | PHASE1 |
Chemical Information
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CAS No. 9008-02-0
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Appearance Solid
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Color Brown to reddish brown
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SMILES
[Hemoglobin]
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
Please store the product under the recommended conditions in the Certificate of Analysis.
Publications (4)
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Journal Impact Factor
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Most Recent
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Int J Biol Macromol
Dynamic catalytic domain plasticity governs substrate specificity in industrial serine proteases: Structural and functional implications. [Abstract]2025 Oct 17;331(Pt 1):148374. PMID: 41110577 -
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Antioxid Redox Signal
Hydrogen Attenuates Oxidative Damage via NRF2-Mediated Mitophagy after Subarachnoid Hemorrhage. [Abstract]2025 Dec 26. PMID: 41468154
Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]
Flow cytometry by Annexin V-APC:7-AAD staining and analysis of apoptosis rate. Hemoglobin (HB) (30 μM; 24 h) treatment increased the percentage of apoptotic cells in HT22 mouse hippocampal neuronal cells, as indicated by higher Annexin V-APC+/7-AAD-cells.
Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]
Western blotting images and quantitative data of relative expression levels of 4-hydroxynonenal (4-HNE), BAX, BCL-2, and cleaved caspase-3 were presented. Hemoglobin (HB) (30 μM; 24 h) treatment upregulated levels of 4-hydroxynonenal (4-HNE), proapoptotic proteins Bax and cleaved caspase-3 while downregulated the antiapoptotic protein BCL-2.
Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]
Hemoglobin (HB) (30 μM; 24 h) exposure led to marked increases in MDA, hydrogen peroxide and decreased superoxide dismutase (SOD) activity.
Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]
Hemoglobin (HB) (30 μM; 24 h) caused the mitochondrial outer membranes to become denser, with some showing rupture, and reduced or eliminated cristae, and induced vacuolization and the occasional formation of autophagic vesicles.
Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]
Western blotting images and quantitative data of relative expression levels of p62, PINK1, PARKIN, and LC3II/I were presented. Hemoglobin (HB) (30 μM; 24 h) increased the LC3-II/I ratio and the levels of PINK1, p62, and Parkin, indicating impaired autophagic flux and enhanced mitophagy activity.
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Int Immunopharmacol
The mechanism study of isoorientin regulating neuroinflammation after subarachnoid hemorrhage through AKT/GSK3β. [Abstract]2026 Apr 1:174:116299. PMID: 41671619
Solvent & Solubility
H2O : 100 mg/mL (Need ultrasonic)
Purity & Documentation
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Data Sheet (270 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
References
[1]. Ahmed MH, Ghatge MS, Safo MK. Hemoglobin: Structure, Function and Allostery. Subcell Biochem. 2020;94:345-382. [Content Brief]
[2]. Ciaccio C, et al. Role of hemoglobin structural-functional relationships in oxygen transport. Mol Aspects Med. 2022 Apr;84:101022. [Content Brief]
[3]. Otterbein L, et al. Hemoglobin provides protection against lethal endotoxemia in rats: the role of heme oxygenase-1. Am J Respir Cell Mol Biol. 1995 Nov;13(5):595-601. [Content Brief]
[4]. Olsson MG, et al. Up-regulation of alpha1-microglobulin by hemoglobin and reactive oxygen species in hepatoma and blood cell lines. Free Radic Biol Med. 2007 Mar 15;42(6):842-51. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)