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51290

Sigma-Aldrich

Hemoglobin from bovine blood

lyophilized, 2×cryst., ≥90% (SDS-PAGE), powder

Synonym(s):

Bovine hemoglobin, Hb, Methemoglobin

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202

biological source

bovine blood

Quality Level

Assay

≥90% (SDS-PAGE)

form

powder

quality

2×cryst.
lyophilized

mol wt

Mr ~64500

technique(s)

UV/Vis spectroscopy: suitable

impurities

salt, none detected
~0.3% Fe

loss

≤8% loss on drying

UniProt accession no.

storage temp.

2-8°C

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General description

Hemoglobin (Hb) is the protein responsible for storage and transport of oxygen and other gaseous ligands in red blood cells (RBC). Hb is also the pioneer material for synthesis of Hb-based oxygen carriers (HBOCs) that can be used as substitutes for RBC.

Application

The solubility of α-elastin has been applied to construction of elastin-mimetic biomaterials.

Biochem/physiol Actions

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.

Other Notes

Review: Oxygen carrier proteins
Sales restrictions may apply

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Paul W Buehler et al.
Biomaterials, 31(13), 3723-3735 (2010-02-13)
Hemoglobin-based oxygen carriers (HBOC) are currently being developed as red blood cell (RBC) substitutes for use in transfusion medicine. Despite significant commercial development, late stage clinical results of polymerized hemoglobin (PolyHb) solutions hamper development. We synthesized two types of PolyHbs
M. Brunori et al.
Topics in Molecular and Structural Biology, 7, 263-263 (1985)
R Bokiniec et al.
Advances in medical sciences, 57(2), 348-355 (2012-11-20)
The aim of this study was to determine brain oxygenation in full-term and preterm neonates using near infrared spectroscopy. A total of 88 full-term and preterm newborn infants without hypoxic-ischaemic disorders admitted to the NICU were examined using NIRS on
Jae G Kim et al.
Journal of biomedical optics, 17(10), 105005-105005 (2012-12-12)
Noninvasive near infrared spectroscopy measurements were performed to monitor cyanide (CN) poisoning and recovery in the brain region and in foreleg muscle simultaneously, and the effects of a novel CN antidote, sulfanegen sodium, on tissue hemoglobin oxygenation changes were compared
Enrico Bucci et al.
Biochemistry, 52(24), 4149-4156 (2013-05-29)
Hill's plots of oxygen binding isotherms reveal the presence of a transition between two different oxygen affinities at the beginning and end of the isotherm. They correspond to the two conformations anticipated by the MWC model, namely, the T and

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