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Merck
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Key Documents

G5009

Sigma-Aldrich

γ-Globulins from bovine blood

≥99% (agarose gel electrophoresis)

Sinónimos:

Bovine γ-Globulin

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About This Item

Número de CAS:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine blood

Quality Level

assay

≥99% (agarose gel electrophoresis)

form

powder

composition

NaCl, ≤4%

technique(s)

enzyme immunoassay: suitable

solubility

0.9% NaCl: soluble 25 mg/mL

storage temp.

−20°C

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General description

Bovine gamma globulin (BGG) is an important component of the immune system of cows and other bovines. BGG is found in the blood of bovines and is primarily used in the production of medical products such as vaccines, serums, and diagnostic reagents. BGG can also be used to treat certain medical conditions, such as hepatitis B, as well as to boost immunity in humans and other animals.

Application

Bovine γ-globulins were used to study the constituents and pH changes in protein rich hyaluronan solution which affect the biological properties of artificial articular joints. It is also used to determine immunoglobulin G in bovine colostrum and milk using direct biosensor SPR-immunoassay.
Bovine γ-globulin has been used as an immunological challenge in studies of mechanisms of immunotolerance.

Biochem/physiol Actions

The γ-G globulins of bovine serum are categorized by anion exchange chromatography, immunoelectrophoresis, zone electrophoresis, ultracentrifugation, and analysis of the products of papain digestion. They have properties similar to analogous components of human serum. This was determined by the methods such as: gel filtration, immunoelectrophoresis, anion exchange chromatography, ultracentrifugation, and reduction with mercaptoethanol. Fast and slow γ-G globulins were classified on the basis of differences in electrophoretic migration rates, chromatographic elution positions, and biological activities (complement fixation). Bovine γ-A was conditionally found in immunoelectrophoretic analyses of serum and chromatographic fractions.

Preparation Note

Prepared from Cohn Fraction II, III

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Harvey E Indyk et al.
Journal of AOAC International, 86(2), 386-393 (2003-05-02)
An automated biosensor surface-plasmon resonance-based assay was developed for the determination of immunoglobulin G (IgG) in bovine milk and colostrum with either goat or rabbit antibovine IgG or protein G used as detecting molecule. The method is configured as a
Marc-Olivier Montjovent et al.
Bioanalysis, 9(18), 1385-1393 (2017-09-29)
Recombinant glycoprotein produced in nonhuman mammalian cell lines can be modified with the immunogenic nonhuman sialic N-glycolylneuraminic acid (Neu5Gc). We describe here a validated method for detection of antidrug antibodies against both protein and Neu5Gc-containing glycan epitopes. An electrochemiluminescent method
Rui Fang et al.
eLife, 11 (2022-01-21)
The ring-like ATPase complexes in the AAA+ family perform diverse cellular functions that require coordination between the conformational transitions of their individual ATPase subunits (Erzberger and Berger, 2006; Puchades et al., 2020). How the energy from ATP hydrolysis is captured
S M Moreira et al.
Ecotoxicology and environmental safety, 73(5), 893-899 (2010-04-30)
This study proposes short-term sublethal assays for the tropics using the fish Poecilia reticulata. Assays were evaluated under realistic exposure scenarios by simulating a runoff over an agricultural area sprayed with deltamethrin (Decis). In situ assays were performed inside microcosms
Emmanuelle V LeBlanc et al.
Current protocols, 1(1), e17-e17 (2021-01-24)
Fungi infect over a billion people worldwide and contribute substantially to human morbidity and mortality despite all available therapies. New antifungal drugs are urgently needed. Decades of study have revealed numerous protein targets of potential therapeutic interest for which potent

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