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Key Documents

AG711-M

Sigma-Aldrich

Human IgG, Polyclonal

Synonym(s):

IgG from Human

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160405
NACRES:
NA.41

biological source

human

Quality Level

antibody form

serum

manufacturer/tradename

Chemicon®

target post-translational modification

unmodified

General description

Immunoglobulin G (IgG) is the most common type of immunoglobulin present in human serum. It has the longest serum half-life compared to other immunoglobulins. IgG contains two equivalent light chains and two identical heavy chains.

Biochem/physiol Actions

Immunoglobulin G (IgG) aids in secondary immune responses. This is the only immunoglobulin type that can cross the placenta. IgG plays a major role in defense mechanisms against local and systemic infections. Polyclonal antibodies from mammalian sources has application in diagnosis.

Physical form

Format: Purified
Liquid in 0.01M PBS, filtered bt 0.45 μm.

Storage and Stability

Store at -20°C until opened. After opening dilute only enough product for a single day′s use. Store remainder at 4°C under sterile conditions for up to six months.

Other Notes

Concentration: Noted on individual vial.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2


Certificates of Analysis (COA)

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CHAPTER 10 - Immunology
FABAD Journal of Pharmaceutical Sciences (2020)
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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