SAB3701172
Anti-Mouse IgG1 (γ-chain specific)-Alkaline Phosphatase antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
ALP, Alk Phos
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.46
biological source
rabbit
Quality Level
conjugate
alkaline phosphatase conjugate
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
mouse
concentration
1.0 mg/mL
technique(s)
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable
shipped in
wet ice
storage temp.
2-8°C
target post-translational modification
unmodified
Related Categories
General description
Antibody format: IgG
Immunoglobulin G (IgG) belongs to the immunoglobulin family and is a widely expressed serum antibody. It consists of a γ heavy chain in the constant (C) region. The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa, respectively. The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. IgG1 is induced due to antibody responses to membrane proteins and soluble protein antigens. It is the most abundant subclass of IgG.
Immunogen
Mouse IgG1 heavy chain
Application
Anti-Mouse IgG1 (γ-chain specific)-Peroxidase antibody produced in rabbit has been used in ELISA.
Biochem/physiol Actions
This product was prepared from monospecific antiserum by immunoaffinity chromatography using antigens coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Alkaline Phosphatase (calf intestine) and Anti-Rabbit Serum. Specificity was confirmed by ELISA at less than 1% cross reactivity against other Mouse heavy or light chain isotypes.
Physical form
Supplied in 0.05 M Tris Chloride, 0.15M Sodium Chloride, 0.001M Magnesium Chloride, 0.0001M Zinc Chloride, 50% (v/v) Glycerol; pH 8.0 with 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free
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.
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Evaluation of vaccinal effectiveness of preparations containing membrane antigens of Leishmania (L.) amazonensis in experimental cutaneous leishmaniasis model
Jo?o G.Ribeiro
International Immunopharmacology, 47, 227-230 (2017)
João G Ribeiro et al.
International immunopharmacology, 47, 227-230 (2017-04-24)
American tegumentary leishmaniasis (ATL) is considered a neglected disease, for which an effective vaccine or an efficient diagnosis is not yet available and whose chemotherapeutic arsenal is threatened by the emergence of resistance by etiological agents such as Leishmania amazonensis.
Human placental Fc receptors and the transmission of antibodies from mother to fetus.
Simister NE and Story CM
Journal of Reproductive Immunology, 37(1), 1-23 (1997)
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
Antibody structure, instability, and formulation.
Wang W
Journal of Pharmaceutical Sciences, 96(1), 1-26 (2007)
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