Skip to Content
Merck
All Photos(1)

Documents

51290

Sigma-Aldrich

Hemoglobin from bovine blood

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

Synonym(s):

Bovine hemoglobin, Hb, Methemoglobin

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202

biological source

bovine blood

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

Looking for similar products? Visit Product Comparison Guide

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
Xiao-Su Hu et al.
Journal of biomedical optics, 18(1), 17003-17003 (2013-01-08)
The reduction of trial-to-trial variability (TTV) in task-evoked functional near-infrared spectroscopy signals by considering the correlated low-frequency spontaneous fluctuations that account for the resting-state functional connectivity in the brain is investigated. A resting-state session followed by a task-state session of
Toru Yamada et al.
PloS one, 7(11), e50271-e50271 (2012-11-28)
In conventional functional near-infrared spectroscopy (fNIRS), systemic physiological fluctuations evoked by a body's motion and psychophysiological changes often contaminate fNIRS signals. We propose a novel method for separating functional and systemic signals based on their hemodynamic differences. Considering their physiological
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service