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Hemoglobin

4 Cited Publications
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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.

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  • Hemoglobin Chemical Structure
    Hemoglobin Chemical Structure
  • Experimental Validation Results for Hemoglobin
  • Experimental Validation Results for Hemoglobin
  • Experimental Validation Results for Hemoglobin
  • Experimental Validation Results for Hemoglobin
  • Experimental Validation Results for Hemoglobin
No. CAS: 9008-02-0
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  • Hemoglobin Chemical Structure
    Hemoglobin Chemical Structure
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    Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]

    Customer Validation
     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.

  • 1/16

    Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]

    Customer Validation
     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.

  • 1/16

    Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]

    Customer Validation
     Hemoglobin (HB) (30 μM; 24 h) exposure led to marked increases in MDA, hydrogen peroxide and decreased superoxide dismutase (SOD) activity.

  • 1/16

    Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]

    Customer Validation
     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.

  • 1/16

    Hemoglobin purchased from MedChemExpress. Usage Cited in: Antioxid Redox Signal. 2025 Dec 26. [Abstract]

    Customer Validation
     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.

  • Hemoglobin