H2625
Hemoglobin from bovine blood
suitable for protease substrate, substrate powder
동의어(들):
Bovine hemoglobin, Hb, Methemoglobin
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
Form:
substrate powder
Biological source:
bovine blood
Mol wt:
Mr ~64500
biological source
bovine blood
Quality Level
form
substrate powder
mol wt
Mr ~64500
technique(s)
activity assay: suitable
solubility
H2O: soluble 20 mg/mL
suitability
suitable for protease substrate
storage temp.
2-8°C
Gene Information
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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 a globular protein with α and β chains with every 141 and 146 amino acids respectively. It exists as a tetramer with each monomer having heterocyclic porphyrin ring with iron constituting the heme.
Application
Hemoglobin from bovine blood has been used as a substrate in cathepsin D activity assay. It has also been used to measure the activity of acid proteases (pepsin-like) in the stomach extract.
The solubility of α-elastin has been applied to construction of elastin-mimetic biomaterials.
Biochem/physiol Actions
Bovine hemoglobin is used in the production of hemoglobin-vesicles (HbV). It has high thermal stability and high oxygen affinity when compared to human hemoglobin. Bovine hemoglobin interacts with synthetic and azo dyes. Polymerized forms of bovine hemoglobin are used to treat autoimmune hemolytic anemia.
Oxygen transporter, NO scavenger
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.
Preparation Note
Prepared from washed, lysed and dialyzed erythrocytes.
Disclaimer
Since native hemoglobin is readily oxidized in air, these preparations may be predominantly methemoglobin.
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
P John Wright et al.
Journal of the American Society for Mass Spectrometry, 20(3), 484-495 (2008-12-23)
The conformations of gas-phase ions of hemoglobin, and its dimer and monomer subunits have been studied with H/D exchange and cross section measurements. During the H/D exchange measurements, tetramers undergo slow dissociation to dimers, and dimers to monomers, but this
Circadian cycle of digestive enzyme production at fasting and feeding conditions in Nile tilapia, Oreochromis niloticus (Actinopterygii: Perciformes: Cichlidae)
MEJIA, MAGNOLIA MONTOYA and others
Acta ichthyologica et piscatoria, 32(2), 188-193 (2016)
High pressure effects on the activities of cathepsins B and D of mackerel and horse mackerel muscle
Fidalgo L, et al.
Czech Journal of Food Sciences, 32(2), 188-193 (2016)
Characteristics of bovine hemoglobin as a potential source of hemoglobin-vesicles for an artificial oxygen carrier
Sakai H, et al.
Journal of Biochemistry, 131(4), 611-617 (2002)
Xianbo Lu et al.
Biosensors & bioelectronics, 23(8), 1236-1243 (2007-12-18)
Carbon nanofibers (CNFs), with typical diameters of approximately 80 nm and lengths of the order of micrometers, are extremely attractive in bioanalytical area as they can combine properties of high surface area, non-toxicity, acceptable biocompatibility, ease of fabrication, chemical and
프로토콜
This procedure may be used for determination of Pepsin activity using hemoglobin as the substrate. It is a spectrophotometric stop rate determination.
Proteinase K activity measured via spectrophotometry using hemoglobin substrate, crucial for enzyme characterization.
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