H1643
Anti-Hamster IgG (whole molecule) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
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About This Item
Produits recommandés
Source biologique
rabbit
Conjugué
unconjugated
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
secondary antibodies
Clone
polyclonal
Forme
buffered aqueous solution
Technique(s)
indirect ELISA: 1:100,000
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Description générale
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.
Actions biochimiques/physiologiques
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.
Forme physique
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide as preservative
Clause de non-responsabilité
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.
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Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
nwg
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Vinay Kumar et al.
JACC. Basic to translational science, 7(10), 1038-1049 (2022-11-08)
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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