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A2064

Sigma-Aldrich

Anti-Human IgG−Alkaline Phosphatase antibody, Mouse monoclonal

clone GG-5, purified from hybridoma cell culture

Synonyme(s) :

Monoclonal Anti-Human IgG (γ-chain specific)

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

mouse

Conjugué

alkaline phosphatase conjugate

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

secondary antibodies

Clone

GG-5, monoclonal

Forme

buffered aqueous glycerol solution

Espèces réactives

human

Technique(s)

direct ELISA: 1:50,000
dot blot: 1:80,000
immunohistochemistry: suitable
western blot (chemiluminescent): 1:80,000

Isotype

IgG1

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

Binds human IgG; does not bind other human Igs.The antibody is specific for a determinant on the heavy chain of human IgG. This antibody will form antigen-antibody complexes in the liquid phase in the presence of 3% PEG 6000.
Human IgGs are glycoprotein antibodies that contain two equivalent light chains and a pair of identical heavy chains. IgGs have four distinct isoforms, ranging from IgG1 to IgG4. These antibodies regulate immunological responses to allergy and pathogenic infections. IgGs have also been implicated in complement fixation and autoimmune disorders.
Monoclonal Anti-Human IgG (Γ-chain specific) (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.

Application

Anti-Human IgG- Alkaline Phosphatase antibody, Mouse monoclonal has been used in:
  • enzyme linked immunosorbent assay (ELISA)
  • western blotting
  • dot blot
  • immunohistology

Elisa assays were performed using alkaline phosphatase conjugated monoclonal mouse anti-human IgG to detect antibodies against various S. Aureus antigens in the serum from healthy individuals. The antibody was diluted 1:30000 in PBSt and incubated with samples for 2 hours at 37 degrees. Reactin was developed using p-nitrophenyl phosphate substrate (Sigma).

Forme physique

Solution in 0.05 M Tris buffer, pH 8.0, containing 1 mM MgCl2, 1% bovine serum albumin, 50% glycerol, and 15 mM sodium azide.

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

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Safety and Immunogenicity of a Pseudomonas aeruginosa Hybrid Outer Membrane Protein F-I Vaccine in Human Volunteers
Mansouri E, et al.
Infection and Immunity, 67(7), 1461-1470 (1999)
George J Broze
Blood cells, molecules & diseases, 52(2-3), 116-120 (2013-10-01)
Acquired factor X (FX) deficiency unrelated to amyloidosis is a rare disorder in which an anti-FX antibody is infrequently detected. A patient with severe bleeding due to a calcium ion-dependent anti-FX IgG antibody is described. The FX affinity purified IgG
Receptor-mediated targeting of spray-dried lipid particles coformulated with immunoglobulin and loaded with a prototype vaccine
Bot AI, et al.
Pharmaceutical Research, 18(7), 971-979 (2001)
Werner E G Müller et al.
Journal of cell science, 128(11), 2202-2207 (2015-04-25)
Polyphosphate (polyP) is a physiologically occurring polyanion that is synthesized especially in bone-forming osteoblast cells and blood platelets. We used amorphous polyP nanoparticles, complexed with Ca(2+), that have a globular size of ∼100 nm. Because polyP comprises inorganic orthophosphate units
Camila A Wilkens et al.
PloS one, 10(3), e0119053-e0119053 (2015-03-15)
Cell engineering has been used to improve animal cells' central carbon metabolism. Due to the central carbon metabolism's inefficiency and limiting input of carbons into the TCA cycle, key reactions belonging to these pathways have been targeted to improve cultures'

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