A0293
Anti-Human IgG (Fab specific)−Peroxidase antibody produced in goat
affinity isolated antibody
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Synonym(s):
Anti Human Fab Antibody, Anti Human Fab Antibody - Anti-Human IgG (Fab specific)-Peroxidase antibody produced in goat
Recommended Products
biological source
goat
Quality Level
conjugate
peroxidase conjugate
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
species reactivity
human
technique(s)
direct ELISA: 1:40,000
dot blot: 1:100,000
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:200
western blot (chemiluminescent): 1:100,000
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Related Categories
General description
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,.
Antibody is isolated from anti-human IgG antiserum by immunospecific purification to remove essentially all goat serum proteins, including immunoglobulins, which do not specifically bind to the Fab fragment of human IgG. Anti-Human IgG is conjugated to peroxidase and then further purified to remove unconjugated material.
Antibody is isolated from anti-human IgG antiserum by immunospecific purification to remove essentially all goat serum proteins, including immunoglobulins, which do not specifically bind to the Fab fragment of human IgG. Anti-Human IgG is conjugated to peroxidase and then further purified to remove unconjugated material.
Immunogen
Fab fragment of human IgG
Application
Anti-Human IgG (Fab specific)-Peroxidase antibody produced in goat has been used in:
Anti-Human IgG antibody was used at a 1:10,000 dilution in PBS and incubated for 1 hour at room temperature. Binding in ELISA assays was detected with a O-phenylene-diamine substrate solution (Sigma).
- western blot
- direct enzyme linked immunosorbent assay (ELISA) at 1:40,000 dilution for analysis of yeast cultures genetically modified to produced recombinant Fab fragments.
- immunohistochemistry
- dot blot
- immunohistochemistry (formalin-fixed, paraffin-embedded sections, 1:200)
Anti-Human IgG antibody was used at a 1:10,000 dilution in PBS and incubated for 1 hour at room temperature. Binding in ELISA assays was detected with a O-phenylene-diamine substrate solution (Sigma).
Goat anti-human IgG (Fab specific)-peroxidase antibody can be used for direct ELISA (1:40,000), dot blot and immunohistochemistry (formalin-fixed, paraffin-embedded sections, 1:200) applications.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT
Preparation Note
Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).
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.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Skin Sens. 1
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Deng Ning et al.
Journal of biochemistry, 134(6), 813-817 (2004-02-11)
Anti-HBs Fab fragment has considerable potential for use in the prevention and treatment of liver diseases by HBV. Here we established a high-level expression system to directly produce anti-HBs Fab fragment in Pichia pastoris. This was achieved by co-integration of
Kristell Lebozec et al.
mAbs, 9(6), 945-958 (2017-06-10)
Glycoprotein VI is a platelet-specific collagen receptor critical for in vivo formation of arterial thrombosis. It is also considered as an attractive target for the development of anti-thrombotic drugs because blocking glycoprotein (GP)VI inhibits platelet aggregation without inducing detrimental effects
James Duehr et al.
mSphere, 3(1) (2018-02-13)
Recent reports in the scientific literature have suggested that anti-dengue virus (DENV) and anti-West Nile virus (WNV) immunity exacerbates Zika virus (ZIKV) pathogenesis in vitro and in vivo in mouse models. Large populations of immune individuals exist for a related
Metabolic responses of CHO cells to limitation of key amino acids
Duarte TM, et al.
Biotechnology and Bioengineering, 111(10), 2095-2106 (2014)
An immuno-assay to quantify influenza virus hemagglutinin with correctly folded stalk domains in vaccine preparations
Rajendran M, et al.
PLoS ONE, 13(4), e0194830-e0194830 (2018)
Articles
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