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SRE0011

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γ-Globulins from bovine blood

Suitable for manufacturing of diagnostic kits and reagents, ≥99% (agarose gel electrophoresis)

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Synonym(s):
Bovine γ-Globulin
CAS Number:
9007-83-4
EC Number:
232-706-1
MDL number:
MFCD00163150
NACRES:
NA.32

Quality Level

400

Assay

≥99% (agarose gel electrophoresis)

form

powder

composition

NaCl, ≤4%

application(s)

diagnostic assay manufacturing

shipped in

wet ice

storage temp.

−20°C

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This Item
G5009G7516G9513
γ-Globulins from bovine blood Suitable for manufacturing of diagnostic kits and reagents, ≥99% (agarose gel electrophoresis)

Sigma-Aldrich

SRE0011

γ-Globulins from bovine blood

γ-Globulins from bovine blood ≥99% (agarose gel electrophoresis)

Sigma-Aldrich

G5009

γ-Globulins from bovine blood

γ-Globulins from bovine blood ≥97% (agarose gel electrophoresis)

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G7516

γ-Globulins from bovine blood

γ-Globulins from goat ≥99% (agarose gel electrophoresis)

Sigma-Aldrich

G9513

γ-Globulins from goat

form

powder

form

powder

form

powder

form

powder

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

-

application(s)

-

shipped in

wet ice

shipped in

-

shipped in

-

shipped in

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

400

Quality Level

-

Quality Level

-

Quality Level

-

General description

γ-Globulins are immunoglobulins that contain IgM, IgA, and IgY. They are glycoproteins produced by plasma cells. The immunoglobulins are heterodimeric molecules comprising two light chains and two heavy chains linked together by disulfide bonds.
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

γ-Globulins from bovine blood has been used along with polyethylene glycol (PEG) to investigate the kinetics of liquid-liquid phase separation (LLPS) in its temporary and arrested state. It has also been used as a parent solution to prevent bacterial growth and study the antibody system with LLPS and highly elevated protein concentrations in arrested transition.
Bovine γ-globulin has been used as an immunological challenge in studies of mechanisms of immunotolerance.

Biochem/physiol Actions

Immunoglobulins are implicated in the activation of the complement system and the opsonization of microbes for phagocytosis. It is also involved in the neutralization of toxins and viruses and blocks the attachment of microbes to mucosal surfaces. They protect our bodies against fungi, viruses, and bacteria. Immunodeficiency is associated with recurrent infectious diseases. 

Preparation Note

Prepared from Cohn Fraction II, III

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Stefano Da Vela et al.
Soft matter, 13(46), 8756-8765 (2017-11-14)
We investigate the transition of the phase separation kinetics from a complete to an arrested liquid-liquid phase separation (LLPS) in mixtures of bovine γ-globulin with polyethylene glycol (PEG). The solutions feature LLPS with upper critical solution temperature phase behavior. At
Justiz Vaillant AA, et al.
Immunoglobulin (2021)
Anita Girelli et al.
Molecular pharmaceutics, 18(11), 4162-4169 (2021-10-13)
Antibody therapies are typically based on high-concentration formulations that need to be administered subcutaneously. These conditions induce several challenges, inter alia a viscosity suitable for injection, sufficient solution stability, and preservation of molecular function. To obtain systematic insights into the
Blood
Sturkie's Avian Physiology, 167-191, 167-191 (2015)
Harry W Schroeder et al.
The Journal of allergy and clinical immunology, 125(2 Suppl 2), S41-S52 (2010-03-05)
Immunoglobulins are heterodimeric proteins composed of 2 heavy and 2 light chains. They can be separated functionally into variable domains that bind antigens and constant domains that specify effector functions, such as activation of complement or binding to Fc receptors.

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