Unfortunately, the solution stability of this material at 2-8°C has not been determined. However, solutions may be stored in aliquots at -20°C for up to 3 months.
H2625
Hemoglobin from bovine blood
suitable for protease substrate, substrate powder
Synonym(s):
Bovine hemoglobin, Hb, Methemoglobin
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About This Item
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biological source
bovine blood
Quality Level
form
substrate powder
mol wt
Mr ~64500
technique(s)
activity assay: suitable
solubility
H2O: soluble 20 mg/mL
suitability
suitable for protease substrate
storage temp.
2-8°C
Gene Information
cow ... HBA1(281221) , HBB(280813) , HBE2(513240) , HBE4(513108) , HBG(511735) , alpha globin(512439)
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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%.[1] Hemoglobin is a globular protein with α and β chains with every 141 and 146 amino acids respectively. It exists as a tetramer with each monomer having heterocyclic porphyrin ring with iron constituting the heme.[2]
Hemoglobin is the major component of red blood cells, and is responsible for their red color. Its normal concentration in erythrocytes is 34%. 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.
Application
Hemoglobin from bovine blood has been used as a substrate in cathepsin D activity assay.[3][4] It has also been used to measure the activity of acid proteases (pepsin-like) in the stomach extract.[5]
The solubility of α-elastin has been applied to construction of elastin-mimetic biomaterials.
Biochem/physiol Actions
Bovine hemoglobin is used in the production of hemoglobin-vesicles (HbV). It has high thermal stability and high oxygen affinity when compared to human hemoglobin.[6] Bovine hemoglobin interacts with synthetic and azo dyes.[2] Polymerized forms of bovine hemoglobin are used to treat autoimmune hemolytic anemia.[7]
Oxygen transporter. The Fe2+/Fe3+ balance is a physiological indicator of blood oxygenation; deoxygenated hemoglobin accessorizes a feedback loop by reducing nitrite to NO, a vasodilator which enhances blood flow to oxygen-deprived tissues.
Caution
Since native hemoglobin is readily oxidized in air, these preparations may be predominantly methemoglobin.
Preparation Note
Prepared from washed, lysed and dialyzed erythrocytes.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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High pressure effects on the activities of cathepsins B and D of mackerel and horse mackerel muscle
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Czech Journal of Food Sciences, 32(2), 188-193 (2016)
P John Wright et al.
Journal of the American Society for Mass Spectrometry, 20(3), 484-495 (2008-12-23)
The conformations of gas-phase ions of hemoglobin, and its dimer and monomer subunits have been studied with H/D exchange and cross section measurements. During the H/D exchange measurements, tetramers undergo slow dissociation to dimers, and dimers to monomers, but this
Luke J Norbury et al.
Biochimie, 93(3), 604-611 (2010-12-21)
Cathepsin proteases are promising vaccine or drug targets for prophylaxis or therapy against Fasciola parasites which express cathepsin L and B proteases during their development. These proteases are believed to be involved in important functions for the parasite, including excystment
A study of the interaction of bovine hemoglobin with synthetic dyes using spectroscopic techniques and molecular docking
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If made up in solution and stored at 2-8C, how long can this product last for?
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Is this product suitable for mammalian cell culture?
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H2625 is specified to be suitable as a substrate in a protease assay. It is not evaluated for cell culture use.
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Do you have any information on purity of this product?
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This product has not been tested for purity. Please see the link below to review the product datasheet:
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/400/152/h2500pis.pdfHelpful?
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