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HEMOGLOBIN

Base Information Edit
  • Chemical Name:HEMOGLOBIN
  • CAS No.:9008-02-0
  • Molecular Formula:C13H10N2O2
  • Molecular Weight:226.2307
  • Hs Code.:3002905150
  • Mol file:9008-02-0.mol
HEMOGLOBIN

Synonyms:Bloodpigments;Hemoglobin;Deoxyhemoglobins;Ferrohemoglobins;Globins, Hbs;Globins, hemo;Haemoglobins;Hbs, deoxy-;Hemoglobins, deoxy-;Reduced Hbs;

Suppliers and Price of HEMOGLOBIN
Supply Marketing:Edit
Business phase:
The product has achieved commercial mass production*data from LookChem market partment
Manufacturers and distributors:
  • Manufacture/Brand
  • Chemicals and raw materials
  • Packaging
  • price
  • Usbiological
  • PSMA2
  • 100ul
  • $ 529.00
  • TRC
  • Hemoglobin Protease Substrate
  • 10g
  • $ 90.00
  • Sigma-Aldrich
  • Hemoglobin from bovine blood
  • 100g
  • $ 207.00
  • Sigma-Aldrich
  • Hemoglobin from bovine blood lyophilized powder
  • 5g
  • $ 142.00
  • Sigma-Aldrich
  • Hemoglobin, Bovine Erythrocytes
  • 5gm
  • $ 116.00
  • Sigma-Aldrich
  • Hemoglobin, Bovine Erythrocytes Hemoglobin,BovineErythrocytes,CAS9008-02-0,isaniron-containingoxygen-tra
  • 5 g
  • $ 111.00
  • Sigma-Aldrich
  • Hemoglobin from bovine blood suitable for microbiology
  • 100 g
  • $ 102.00
  • Sigma-Aldrich
  • Hemoglobin from bovine blood lyophilized powder
  • 10g
  • $ 245.00
  • Sigma-Aldrich
  • Hemoglobin human lyophilized powder
  • 5g
  • $ 225.00
  • Sigma-Aldrich
  • Hemoglobin from bovine blood
  • 1kg
  • $ 1240.00
Total 65 raw suppliers
Chemical Property of HEMOGLOBIN Edit
Chemical Property:
  • Appearance/Colour:solid 
  • PSA:0.00000 
  • LogP:0.00000 
  • Storage Temp.:2-8°C 
  • Solubility.:0.6 M HCl: soluble20mg/mL 
  • Water Solubility.:Soluble in water. 
Purity/Quality:

90%, *data from raw suppliers

PSMA2 *data from reagent suppliers

Safty Information:
  • Pictogram(s): Explosive
  • Hazard Codes:
  • Safety Statements: 22-24/25 
MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:
  • Description Haemoglobin, the oxygen-transport protein in the red blood cells, is a tetramer and each of the four chains contains a haeme group. It is interesting to note that the four haeme groups in haemoglobin do not operate independently. The release (and binding) of oxygen is a cooperative process, which means that the loss (uptake) of the first oxygen molecule triggers the release of the remaining three.The current model for oxygen binding in haemoglobin and myoglobin can be explained in the following way. The deoxy form contains a high-spin Fe(II) centre, which, because of its size, does not form a plane with its four nitrogen donor atoms. Instead, it is located slightly above the plane, drawn towards the His residue. Once oxygen enters trans to the His residue, the iron centre is oxidised to a low-spin Fe3+ centre and O2 is reduced to [O2]-. Both species contain an unpaired electron. The low-spin Fe3+ moves into the plane and pulls the His residue down. This affects the remaining protein chain and triggers the uptake/release of oxygen in the other three haeme groups.
  • Uses Hemoglobin is the most important respiratory protein of vertebrates by virtue of its ability to transport oxygen from the lungs to body tissues, and to facilitate the return transport of carbon dioxide. It is used as a coloring agent for pet foods, a natural source of iron for nutraceuticals, a protein source for non-ruminant animals, and as a raw material for pharmaceutical porphyrin derivative production. Medicine, usually called hemoglobin. Hemoglobin from bovine blood has been used in: standard curve generation for the quantification intraparenchymal hemorrhage and parenchymal hemorrhage in spinal cord homogenate using Drabkin′s assay, Quadrupole-Ion Mobility-Time-of-Flight mass spectrometery the generation of molecularly imprinted polymers (MIPs) to mimic high molecular-weight polyethylene glycol (PEG) in crystallization studies
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