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HEMOGLOBIN

Product Name
HEMOGLOBIN
CAS No.
9008-02-0
Chemical Name
HEMOGLOBIN
Synonyms
MU;HB;GST1;GTH4;GTM1;PMSA2;PSMA2;C01708;HB, BABOON;HEMOGLOBIN
CBNumber
CB3741179
Molecular Formula
C13H10N2O2
Formula Weight
226.2307
MOL File
9008-02-0.mol
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HEMOGLOBIN Property

storage temp. 
2-8°C
solubility 
0.6 M HCl: soluble20mg/mL
form 
substrate powder
color 
Dark brown powder
Water Solubility 
Soluble in water.
EPA Substance Registry System
Hemoglobins (9008-02-0)
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Safety

Hazard Codes 
B
Safety Statements 
22-24/25
WGK Germany 
3
1-10
TSCA 
Yes
HS Code 
3002905150
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Hazard and Precautionary Statements (GHS)

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N-Bromosuccinimide Price

Sigma-Aldrich
Product number
WH0002944M1
Product name
Monoclonal Anti-GSTM1 antibody produced in mouse
Purity
clone 3B10, purified immunoglobulin, buffered aqueous solution
Packaging
100μG
Price
$524
Updated
2024/03/01
Sigma-Aldrich
Product number
3745
Product name
Hemoglobin, Bovine Erythrocytes
Purity
Hemoglobin,BovineErythrocytes,CAS9008-02-0,isaniron-containingoxygen-tra
Packaging
5G
Price
$151
Updated
2024/03/01
Sigma-Aldrich
Product number
08449
Product name
Hemoglobin from bovine blood
Purity
suitable for microbiology
Packaging
100g
Price
$115
Updated
2022/05/15
Sigma-Aldrich
Product number
08449
Product name
Hemoglobin from bovine blood
Purity
suitable for microbiology
Packaging
500g
Price
$412
Updated
2022/05/15
Alfa Aesar
Product number
J63838
Product name
Hemoglobin, bovine
Packaging
5g
Price
$31.8
Updated
2023/06/20
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HEMOGLOBIN Chemical Properties,Usage,Production

Description

Haemoglobin, the oxygen-transport protein in the red blood cells, is a tetramer and each of the four chains contains a haeme group. It is interesting to note that the four haeme groups in haemoglobin do not operate independently. The release (and binding) of oxygen is a cooperative process, which means that the loss (uptake) of the first oxygen molecule triggers the release of the remaining three.
The current model for oxygen binding in haemoglobin and myoglobin can be explained in the following way. The deoxy form contains a high-spin Fe(II) centre, which, because of its size, does not form a plane with its four nitrogen donor atoms. Instead, it is located slightly above the plane, drawn towards the His residue. Once oxygen enters trans to the His residue, the iron centre is oxidised to a low-spin Fe3+ centre and O2 is reduced to [O2]-. Both species contain an unpaired electron. The low-spin Fe3+ moves into the plane and pulls the His residue down. This affects the remaining protein chain and triggers the uptake/release of oxygen in the other three haeme groups.

Uses

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. It is used as a coloring agent for pet foods, a natural source of iron for nutraceuticals, a protein source for non-ruminant animals, and as a raw material for pharmaceutical porphyrin derivative production.

Uses

Medicine, usually called hemoglobin.

Uses

Hemoglobin from bovine blood has been used in:

  • standard curve generation for the quantification intraparenchymal hemorrhage and parenchymal hemorrhage in spinal cord homogenate using Drabkin′s assay, Quadrupole-Ion Mobility-Time-of-Flight mass spectrometery
  • the generation of molecularly imprinted polymers (MIPs) to mimic high molecular-weight polyethylene glycol (PEG) in crystallization studies

Definition

The respiratory protein of the red blood cells, it transfers oxygen from the lungs to the tissues and carbon dioxide from the tissues to the lungs. Its affinity for carbon monoxide is >200 times that for oxygen. Hemoglobin is a conjugated protein of molec

Definition

The pigment of the red blood cells that is responsible for the transport of oxygen from the lungs to the tissues. It consists of a basic protein, globin, linked with four heme groups. Heme is a complex compound containing an iron atom. The most important property of hemoglobin is its ability to combine reversibly with one molecule of oxygen per iron atom to form oxyhemoglobin, which has a bright red color. The iron is present in the divalent state (iron(II)) and this remains unchanged with the binding of oxygen. There are variations in the polypeptide chains, giving rise to different types of hemoglobins in different species. The binding of oxygen depends on the oxygen partial pressure; high pressure favors formation of oxyhemoglobin and low pressure favors release of oxygen.

Definition

One of a group ofglobular proteins occurring widely inanimals as oxygen carriers in blood.Vertebrate haemoglobin comprisestwo pairs of polypeptide chains,known as α-chains and β-chains(forming the globin protein), witheach chain folded to provide a bindingsite for a haem group. Each ofthe four haem groups binds oneoxygen molecule to form oxyhaemoglobin.Dissociation occurs inoxygen-depleted tissues: oxygen is releasedand haemoglobin is reformed.The haem groups also bind other inorganicmolecules, including carbonmonoxide (to form carboxyhaemoglobin).In vertebrates, haemoglobinis contained in the red blood cells(erythrocytes).

General Description

Native hemoglobin from bovine erythrocytes. A major oxygen-transporting component of red blood cells that is also nitric oxide scavenger. Blocks carbachol-stimulated cGMP production. This preparation contains primarily Ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen. Note: this preparation contains primarily ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen.

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.

Purification Methods

Purify it from blood using CM-32 cellulose column chromatography. [Matsukawa et al. J Am Chem Soc 107 1108 1985.] For the purification of the  and  chains see Hill et al. Biochemical Preparations 10 55 1963. Histones (from S4A mouse lymphoma). The purification of histones uses a macroprocess column, heptafluorobutyric acid as solubilising and ion-pairing agent and an acetonitrile gradient. [McCroskey et al. Anal Biochem 163 427 1987.]

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HEMOGLOBIN Suppliers

Kono Chem Co.,Ltd
Tel
029-86107037-8009 13279399072
Fax
13279399072
Email
info@konochemical.com
Country
China
ProdList
741
Advantage
58
Nanjing Dulai Biotechnology Co., Ltd.
Tel
025-84699383-8003 18013301590
Fax
025-84699383-8003
Email
njduly@126.com
Country
China
ProdList
972
Advantage
55
Tongchuan Boliante Chemical Co. LTD
Tel
17719597442
Email
642232259@qq.com
Country
China
ProdList
92
Advantage
58
Kono Chem Co., Ltd
Tel
029-86107037-8014 18292830413
Email
info@konochemical.com
Country
China
ProdList
537
Advantage
58
J & K SCIENTIFIC LTD.
Tel
010-82848833 400-666-7788
Fax
86-10-82849933
Email
jkinfo@jkchemical.com
Country
China
ProdList
96815
Advantage
76
Meryer (Shanghai) Chemical Technology Co., Ltd.
Tel
021-61259108 18621169109
Fax
86-21-61259102
Email
market03@meryer.com
Country
China
ProdList
40240
Advantage
62
TCI (Shanghai) Development Co., Ltd.
Tel
021-67121386
Fax
021-67121385
Email
Sales-CN@TCIchemicals.com
Country
China
ProdList
24539
Advantage
81
Beijing HwrkChemical Technology Co., Ltd
Tel
0757-86329057 18501085097
Fax
010-89508210
Email
sales3.gd@hwrkchemical.com
Country
China
ProdList
7639
Advantage
55
Energy Chemical
Tel
021-021-58432009 400-005-6266
Fax
021-58436166
Email
sales8178@energy-chemical.com
Country
China
ProdList
44700
Advantage
61
Beijing Ouhe Technology Co., Ltd
Tel
010-82967028 13552068683
Fax
+86-10-82967029
Email
2355560935@qq.com
Country
China
ProdList
12458
Advantage
60
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View Lastest Price from HEMOGLOBIN manufacturers

Hebei Guanlang Biotechnology Co., Ltd.
Product
Hemoglobin 9008-02-0
Price
US $0.00-0.00/KG
Min. Order
1KG
Purity
99%
Supply Ability
500000kg
Release date
2022-10-17
Career Henan Chemical Co
Product
HEMOGLOBIN 9008-02-0
Price
US $6.60/KG
Min. Order
1KG
Purity
97%-99%
Supply Ability
1kg -1000kg
Release date
2020-01-02

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