H1643
Anti-Hamster IgG (whole molecule) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
buffered aqueous solution
technique(s)
indirect ELISA: 1:100,000
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Related Categories
General description
IgG is present in large quantities in the human serum. IgG is composed of glycoproteins, out of which it is 82-96% proteins and 4-18% carbohydrates. It consists of four sub-classes i.e IgG1, IgG2, IgG3, and IgG4. IgG is composed of four polypeptide chains-two heavy chains (γ chains) and two light chains (κ or λ chains) which are linked by inter-chain disulfide bonds. The heavy chains consist of a N-terminal variable domain (VH) and three constant domains (CH1, CH2, CH3). A hinge region exists between the CH1 and CH2 region. The light chains have one N-terminal variable domain (VL) and one constant domain (CL). The heavy and the light chains are linked at VH and CH1 domain to form the Fab arm (Fragment antigen binding). The antigen binds to the V regions of the antibody.
Application
Anti-Hamster IgG (whole molecule) antibody produced in rabbit is suitable for use in Immunoelectron Microscopy and FACS.
Biochem/physiol Actions
IgG antibody subtype is the most abundant serum immunoglobulin 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.
IgG, a monoclonal antibody can be cleaved at the hinge region by nonspecific proteases like papain and pepsin. This can result in univalent Fab (Fragment antigen binding) fragments or bivalent F(ab′)2 fragments. These two enzymes have a broad substrate specificity resulting in heterogenous fragments.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide as preservative
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
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Certificates of Analysis (COA)
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Vinay Kumar et al.
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CD4+ T cells turn pathological during heart failure (HF). We show that the expression of tumor necrosis factor (TNF)-α and tumor necrosis factor receptor (TNFR1) increases in HF-activated CD4+ T cells. However, the role of the TNF-α/TNFR1 axis in T-cell
C Reis e Sousa et al.
The Journal of experimental medicine, 178(2), 509-519 (1993-08-01)
Dendritic cells (DC) isolated from lymphoid tissues are generally thought to be nonphagocytic in culture. It has therefore been unclear how these cells could acquire particulate antigens such as microorganisms for initiation of primary immune responses. Lymphoid DC derive in
Sandra L Martínez-Hernández et al.
Journal of immunology research, 2021, 6697900-6697900 (2021-04-08)
Entamoeba histolytica is an intestinal parasite that causes dysentery and amebic liver abscess. E. histolytica has the capability to invade host tissue by union of virulence factor Gal/GalNAc lectin; this molecule induces an adherence-inhibitory antibody response as well as to
Papain digestion of different mouse IgG subclasses as studied by electrospray mass spectrometry
Adamczyk M, et al.
Journal of Immunological Methods, 237(1-2), 95-104 (2000)
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
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