H7379
Hemoglobin human
lyophilized powder
Synonym(s):
Hb
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All Photos(3)
About This Item
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biological source
human
form
lyophilized powder
technique(s)
enzyme immunoassay: suitable
impurities
HIV and hepatitis B antigen, tested negative
solubility
H2O: soluble 20 mg/mL
storage temp.
2-8°C
Gene Information
human ... HBA1(3039) , HBA2(3040) , HBB(3043) , HBD(3045) , HBE1(3046) , HBG1(3047) , HBG2(3048) , HBQ1(3049) , HBZ(3050)
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%. 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 was used in the development of a rapid enzyme immunoassay for the detection of retinol-binding protein. It was also used in the inhibition of human platelet reactivity by endothelium-derived relaxing factor.
Biochem/physiol Actions
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.
Oxygen transporter, NO scavenger
Caution
Since native hemoglobin is readily oxidized in air, these preparations may be predominantly methemoglobin.
Disclaimer
RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Leila Pishkar et al.
Journal of biomolecular structure & dynamics, 35(3), 603-615 (2016-05-07)
In this study, a novel method to probe molecular interactions and binding of human hemoglobin (Hb) with nanodiamond (ND) was introduced based on the surface tension measurement. This method complements conventional techniques, which are basically done by zeta potential and
Mieke Steenbeke et al.
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Nitrosation of a conserved cysteine residue at position 93 in the hemoglobin β chain (β93C) to form S-nitroso (SNO) hemoglobin (Hb) is claimed to be essential for export of nitric oxide (NO) bioactivity by the red blood cell (RBC) to
Rebeca M Torrente-Rodríguez et al.
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S-glutathionylated proteins (GSSP), i.e., protein-mixed disulfides with glutathione (GSH), are considered a suitable biomarker of oxidative stress. In fact, they occur within cells at low level and their concentration increases markedly under pro-oxidant conditions. Plasma is something different, since it
Chromatograms
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