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Hemoglobin equine

lyophilized powder

CAS Number:
MDL number:

biological source


Quality Level


lyophilized powder


protein quantification: suitable


H2O: soluble 10 mg/mL

UniProt accession no.

storage temp.


Gene Information

General description

Hemoglobin is the major component of red blood cells and is responsible for their red color. Its normal concentration in erythrocytes is 34%. The structure of horse hemoglobin was elucidated first. It comprises heme (iron protoporphyrin IX group) and four polypeptide chains. The fetal and adult hemoglobin of horse are structurally identical.


Hemoglobin equine has been used as a standard protein:
  • to test solid-film sampling methodology in Fourier transform infrared spectroscopy (FT-IR) for protein secondary structure determination
  • in capillary reversed-phase liquid chromatography-tandem mass spectrometry (LC/MS/MS) post enzymatic digestion
  • for quantification of hemoglobin content from the planktonic crustacean, Daphnia magna


10 g in poly bottle

Biochem/physiol Actions

Hemoglobin is the most important respiratory protein of vertebrates by its ability to transport oxygen from the lungs to body tissues and to facilitate the return transport of carbon dioxide. The ferrous-ferric (Fe2+/Fe3+) balance is a physiological indicator of blood oxygenation. Deoxygenated hemoglobin accessorizes a feedback loop by reducing nitrite to nitric oxide (NO), a vasodilator which enhances blood flow to oxygen-deprived tissues. The fetal and adult hemoglobin from horse display differences in their affinity towards 2,3-diphosphoglycerate (2,3-DPG). Mutation in the globin gene is implicated in sickle cell anemia.
Oxygen transporter, NO scavenger


Since native hemoglobin is readily oxidized in air, these preparations may be predominantly methemoglobin.

Storage Class Code

13 - Non Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

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Certificate of Origin

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Product Information Sheet

Quotes and Ordering

Yan Zhang et al.
Zoological science, 20(9), 1087-1093 (2003-10-28)
The physiological significance of the position and shape of the oxygen equilibrium curve (OEC) of horse hemoglobin (Hb) is considered from the viewpoint of oxygen (O2) transport efficiency and the effectiveness of the Bohr effect. In horse fetal and maternal
Alain J Marengo-Rowe
Proceedings (Baylor University. Medical Center), 19(3), 239-245 (2007-01-26)
In 1949 Pauling and his associates showed that sickle cell hemoglobin (HbS) belonged to an abnormal molecular species. In 1958 Ingram, who used a two-dimensional system of electrophoresis and chromatography to break down the hemoglobin molecule into a mixture of
A comparative study on STM imaging and electrocatalytic activity of different surfaces modified with flavin adenine dinucleotide
Jingdong Zhang, Qijin Chi, Erkang Wang, Shaojun Dong
Electrochimica Acta, 40, 733-744 (1995)
Alan N Schechter
Blood, 112(10), 3927-3938 (2008-11-08)
Much of our understanding of human physiology, and of many aspects of pathology, has its antecedents in laboratory and clinical studies of hemoglobin. Over the last century, knowledge of the genetics, functions, and diseases of the hemoglobin proteins has been
Junting Zhang et al.
Analytical and bioanalytical chemistry, 409(18), 4459-4465 (2017-05-21)
Fourier transform infrared (FTIR) spectroscopy is one of the widely used vibrational spectroscopic methods in protein structural analysis. The protein solution sample loaded in demountable CaF

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