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Merck
모든 사진(2)

주요 문서

H2625

Sigma-Aldrich

Hemoglobin from bovine blood

suitable for protease substrate, substrate powder

동의어(들):

Bovine hemoglobin, Hb, Methemoglobin

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About This Item

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

생물학적 소스

bovine blood

Quality Level

양식

substrate powder

분자량

Mr ~64500

기술

activity assay: suitable

solubility

H2O: soluble 20 mg/mL

적합성

suitable for protease substrate

UniProt 수납 번호

저장 온도

2-8°C

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일반 설명

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.

애플리케이션

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.

생화학적/생리학적 작용

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.

주의사항

Since native hemoglobin is readily oxidized in air, these preparations may be predominantly methemoglobin.

제조 메모

Prepared from washed, lysed and dialyzed erythrocytes.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


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문서 라이브러리 방문

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)
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)
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)
Luke J Norbury et al.
Biochimie, 93(3), 604-611 (2010-12-21)
Cathepsin proteases are promising vaccine or drug targets for prophylaxis or therapy against Fasciola parasites which express cathepsin L and B proteases during their development. These proteases are believed to be involved in important functions for the parasite, including excystment

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.

Chromatograms

application for HPLC

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