I8635
Anti-Human IgG (whole molecule) antibody produced in rabbit
whole antiserum
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
whole antiserum
antibody product type
secondary antibodies
clone
polyclonal
contains
15 mM sodium azide
technique(s)
indirect ELISA: 1:60,000
quantitative precipitin assay: 2.5 mg/mL
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
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General description
Immunoglobulins (Igs) belongs to the immunoglobulin super-family. There are five different types of Immunoglobulins. Each immunoglobin has two heavy (H) and two light (L) chains, held together by disulphide linkages. Each light chain comprises of one variable N-terminal region and a constant C-terminal region. Heavy chain has one variable N-terminal region and three or four constant (CH1-CH4) C-terminal regions. The four classes of IgG can be IgG1, IgG2, IgG3, and IgG4.
Application
Anti-Human IgG (whole molecule) antibody produced in rabbit has been used in enzyme linked immunosorbent assay.
Biochem/physiol Actions
IgG antibody subtype is the most abundant of serum immunoglobulins of the immune system. It is secreted by B cells and is found in blood and extracellular fluids and provides protection from infections caused by bacteria, fungi and viruses. Maternal IgG is transferred to fetus through the placenta that is vital for immune defense of the neonate against infections.
IgG1 deficiency results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections, IgG3 mediates effector functions and IgG4 is associated with asymptomatic infection. IgG antibodies have enormous therapeutic potential and the Fc region is for the development of therapeutic antibody.
Preparation Note
delipidized
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.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Antibodies reacting with human immunoglobulin in sera from autoimmune thyroid disease patients as a risk factor for false positive results in IgA assessment
Haroun M and El-Masry MH
Central European Journal of Immunology, 33, 208-212 (2008)
Molecular properties of human IgG subclasses and their implications for designing therapeutic monoclonal antibodies against infectious diseases
Irani V, et al.
Molecular Immunology, 67 (2015)
Structure and function of immunoglobulins.
Schroeder Jr H W and Cavacini L
The Journal of Allergy and Clinical Immunology, 125(2), S41-S52 (2010)
Gestur Vidarsson et al.
Frontiers in immunology, 5, 520-520 (2014-11-05)
Of the five immunoglobulin isotypes, immunoglobulin G (IgG) is most abundant in human serum. The four subclasses, IgG1, IgG2, IgG3, and IgG4, which are highly conserved, differ in their constant region, particularly in their hinges and upper CH2 domains. These
S Hashira et al.
Pediatrics international : official journal of the Japan Pediatric Society, 42(4), 337-342 (2000-09-15)
Maternal immunoglobulin G (IgG), transferred across the placenta to the fetus during intrauterine life, is an important component of the neonatal immunological defence mechanisms against infection. There is controversy with respect to differences in placental transfer of the different IgG
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