A2179
Anti-Mouse IgG (Fab specific)–Alkaline Phosphatase antibody produced in goat
affinity isolated antibody, buffered aqueous solution
Synonyme(s) :
Goat Anti-Mouse IgG (Fab specific)–AP
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About This Item
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Source biologique
goat
Conjugué
alkaline phosphatase conjugate
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
secondary antibodies
Clone
polyclonal
Forme
buffered aqueous solution
Espèces réactives
mouse
Ne doit pas réagir avec
horse, human, bovine
Technique(s)
direct ELISA: 1:40,000
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:25
western blot (chemiluminescent): 1:80,000
Conditions d'expédition
wet ice
Température de stockage
2-8°C
Modification post-traductionnelle de la cible
unmodified
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Description générale
Immunoglobulins (Igs) belongs to the immunoglobulin super-family. Each immunoglobin have two heavy (H) and two light (L) chains held together by disulfide linkages.
Immunogène
Purified mouse IgG, Fab fragment
Application
Alkaline phosphatase-conjugated goat anti-mouse IgG (Fab specific) was used as the secondary antibody in ELISA assays to measure the reacitivity of mABs to thyrogobulin peptides. Absorbance was measured at 405 nm.
Anti-Mouse IgG (Fab specific)-Alkaline Phosphatase antibody produced in goat has been used in:
- western blotting
- immunoblotting
- enzyme linked immunosorbent assay (ELISA)
- immunohistochemistry
Actions biochimiques/physiologiques
Digestion of IgG by papain results in generation of fragment antigen binding (Fab) comprising of one complete L chain and a variable and CH1 region of H chain. Pepsin digestion of IgG results in fragment crystallisable (fc), comprises of the H chain constant region. IgG antibody have enormous therapeutic potential and the Fc are is for the development of therapeutic antibody. Although the antibody site is located in the terminal end of the human IgG molecule (part of the Fab fragment), the Fc portion has various important functions such as complement fixation, site for rheumatoid factor (autoantibodies directed to Fc), passage through placental membrane and Staphylococcus protein A binding.
Immunoglobulin G (IgG) is a glycoprotein antibody that regulates immune responses such as phagocytosis and is also involved in the development of autoimmune diseases . Mouse IgGs have four distinct isotypes, namely, IgG1, IgG2a, IgG2b, and IgG3. IgG1 regulates complement fixation in mice .
Autres remarques
Antibody adsorbed with bovine, equine and human serum proteins.
Forme physique
Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2 and 15 mM sodium azide.
Notes préparatoires
Adsorbed to reduce background staining with bovine, horse, or human samples.
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)
WGK 2
Certificats d'analyse (COA)
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Szymon W Manka et al.
Nature chemical biology (2023-01-17)
Recent cryogenic electron microscopy (cryo-EM) studies of infectious, ex vivo, prion fibrils from hamster 263K and mouse RML prion strains revealed a similar, parallel in-register intermolecular β-sheet (PIRIBS) amyloid architecture. Rungs of the fibrils are composed of individual prion protein
Laszlo L P Hosszu et al.
Communications biology, 3(1), 402-402 (2020-07-31)
Prion diseases, a group of incurable, lethal neurodegenerative disorders of mammals including humans, are caused by prions, assemblies of misfolded host prion protein (PrP). A single point mutation (G127V) in human PrP prevents prion disease, however the structural basis for
Szymon W Manka et al.
Nature communications, 13(1), 4004-4004 (2022-07-14)
Mammalian prions propagate as distinct strains and are composed of multichain assemblies of misfolded host-encoded prion protein (PrP). Here, we present a near-atomic resolution cryo-EM structure of PrP fibrils present in highly infectious prion rod preparations isolated from the brains
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Di Stefano A, et al.
The European Respiratory Journal, 20(3), 556-563 (2002)
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