Bilirubin
Cytochrome C
Gastric Mucin
HCG
FSH
UTI
PMSG
Aprotinin
Asparaginase
Beta Glucanase
Bromelain
Chymotrypsin
Kallikrein
Lysozyme
Pancreatin
Papain
Pepsin
Streptokinase
Trypsin
Urokinase
Coenzyme A
Coenzyme A Trilithium
Coenzyme Q10
Beta Glucans
Chitosan
Chondroitin Sulfate
Dextran
Dextran Sulfate Sodium
Glucosamine HCl
Heparin Sodium
Heparinoid
Hyaluronic Acid
Rosemary Extract
Sodium Cholate
Bilirubin
Cytochrome C
Gastric Mucin
HCG
FSH
UTI
PMSG
Aprotinin
Asparaginase
Beta Glucanase
Bromelain
Chymotrypsin
Kallikrein
Lysozyme
Pancreatin
Papain
Pepsin
Streptokinase
Trypsin
Urokinase
Coenzyme A
Coenzyme A Trilithium
Coenzyme Q10
Beta Glucans
Chitosan
Chondroitin Sulfate
Dextran
Dextran Sulfate Sodium
Glucosamine HCl
Heparin Sodium
Heparinoid
Hyaluronic Acid
Rosemary Extract
Sodium Cholate
Jiagen Biotechnologies
Proteins

Hemin

CAS No:16009-13-5
EINECS No:240-654-3
Synonyms:chlorohemin, ferriheme, ferriprotoporphyrin IX chloride, hematin chloride, hemin B, heme chloride, panhematin, protoferriheme, protohemin, iron (III)-protoporphyrin IX chloride

Product Summary

Hemin is a biologically essential heme analog and HO-1 inducer, widely used in research to investigate oxidative stress, iron metabolism, and immune modulation. As a heme source, it reconstitutes or activates hemoproteins and serves in the study of disease mechanisms like anemia, inflammation, and neurodegeneration. Properly stored, Hemin is stable and a powerful tool for both in vitro and in vivo applications.

  • Formula: C34H32N4O4FeCl
  • Formula Molecular Weight: 651.96

Function

Hemin is an iron-containing porphyrin with chlorine. It is the oxidized (Fe3+) form of heme and acts primarily as: A heme oxygenase-1 (HO-1) inducer; a heme source in biochemical systems; an enzyme cofactor, especially for cytochromes; a modulator of oxidative stress and inflammation.

Mechanism of Action

  1. Hemin binds to heme-responsive transcription factors, particularly Bach1, displacing it to activate the expression of HO-1, a cytoprotective enzyme.
  2. It serves as a cofactor for heme-containing enzymes (e.g., cytochrome P450s, catalase, peroxidases).
  3. Hemin can modulate immune responses via regulation of Toll-like receptor pathways.
  4. It exhibits pro-oxidant or antioxidant effects, depending on the biological context and concentration.

Applications in Scientific Research

  • Induction of HO-1 to study antioxidant, anti-inflammatory, and cytoprotective pathways.
  • Cellular heme supplementation in heme-deficient or heme-requiring cell lines.
  • Iron metabolism studies, especially in macrophages, erythropoiesis, or hemolytic models.
  • Drug screening involving heme-binding agents or hemoproteins.
  • Cancer research: Modulation of proliferation and ferroptosis pathways.
  • Neurodegenerative disease studies: Role in oxidative injury and neuroinflammation.
  • Heme-based enzyme reconstitution: e.g., cytochrome c or catalase.
  • Antiviral and antimicrobial research: Hemin can impact immune signaling.

Packaging & Storage

  • Source: porcine or bovine
  • Store at 2 to 8°C.

References

  1. Green D, Ts’ao CH. 1990: Hematin: effects on hemostasis, J Lab Clin Med. 115(2):144-7.
  2. Grenoble DC, Drickamer HG. 1968: The effect of pressure on the oxidation state of iron. 3. Hemin and hematin, Proc Natl Acad Sci U S A. 61(4):1177-82.
  3. Mikhailova DM, et al. 2025: Analysis of ferric protoporphyrin IX effects on human platelets: hematin is a more potent agonist than hemin, Cells. 14(4):255.
  4. Georgiou-Siafis SK, et al. 2022: Glutathione-hemin/hematin adduct formation to disintegrate cytotoxic oxidant hemin/hematin in human K562 cells and red blood cells' hemolysates: Impact of glutathione on the hemolytic disorders and homeostasis, Antioxidants (Basel). 11(10):1959.
  5. Herrera J, et al. 2023: Revising the formation of β-hematin crystals from hemin in aqueous-acetate medium containing chloroquine: modeling the kinetics of crystallization and characterizing their physicochemical properties, Cryst Growth Des. 7:4791–806.
  6. Bohle DS, Helms JB. 1993: Synthesis of beta-hematin by dehydrohalogenation of hemin, Biochem Biophys Res Commun. 193(2):504-8.
  7. Berger BJ, et al. 1995: High-performance liquid chromatographic analysis of biological and chemical heme polymerization, Anal Biochem. 231(1):151-6.
  8. Mikhailova DM, et al. 2024: Hematin- and Hemin-Induced Spherization and Hemolysis of Human Erythrocytes Are Independent of Extracellular Calcium Concentration, Cells. 13(6):554.
  9. Herrera J, et al. 2025: Distinct physical properties of β-hematin in two synthetic media: compelling evidence, ACS Omega. 10(12):11770-85.
  10. Yu Q, et al. 2024: Intestinal-targeted digestion of heme chloride by forming inclusion complexes in vitro, Foods. 13(19):3078.
  11. Liu J, et al. 2025: Dual-signal biosensor based on G-quadruplex/hemin DNAzyme and zinc-doped molybdenum disulfide quantum dots for ultrasensitive detection of tumor biomarker, Talanta. 283:127179.
  12. Bacchella C, et al. 2025: Hemin, copper and amyloid-β: A medley involved in Alzheimer's disease. An interaction that fine regulates the reactivity, J Inorg Biochem. 263:112775.

Jiagen Biotechnologies supplies quality Hemin of various specifications.
Contact us at sales@jiagen.ca to place an order.

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