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Key Documents

H7379

Sigma-Aldrich

Hemoglobin human

lyophilized powder

Synonym(s):

Hb

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
eCl@ss:
42030116
NACRES:
NA.61

Pricing and availability is not currently available.

biological source

human

Quality Level

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

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.[1] It was also used in the inhibition of human platelet reactivity by endothelium-derived relaxing factor.[2]

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


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    Mieke Steenbeke et al.
    Clinical chemistry and laboratory medicine, 58(10), 1759-1767 (2020-07-11)
    Objectives In this study, the possibilities of Fourier-transformed infrared spectroscopy (FTIR) for analysis of urine sediments and for detection of bacteria causing urinary tract infections (UTIs) were investigated. Methods Dried urine specimens of control subjects and patients presenting with various
    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
    Chiao-Wang Sun et al.
    Circulation, 139(23), 2654-2663 (2019-03-25)
    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.
    PloS one, 12(4), e0175056-e0175056 (2017-04-05)
    The first electrochemical immunosensor for the determination of fibroblast growth factor receptor 4 (FGFR4) biomarker is reported in this work. The biosensor involves a sandwich configuration with covalent immobilization of a specific capture antibody onto activated carboxylic-modified magnetic microcarriers (HOOC-MBs)
    Nai-Jia Huang et al.
    Nature communications, 8(1), 423-423 (2017-09-06)
    A short half-life in the circulation limits the application of therapeutics such as single-domain antibodies (VHHs). We utilize red blood cells to prolong the circulatory half-life of VHHs. Here we present VHHs against botulinum neurotoxin A (BoNT/A) on the surface

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