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Anti-Human IgG (Fc specific)−FITC antibody, Mouse monoclonal

clone HP-6017, purified from hybridoma cell culture

Monoclonal Anti-Human IgG (Fc specific)

origen biológico



FITC conjugate

forma del anticuerpo

purified from hybridoma cell culture

antibody product type

secondary antibodies


HP-6017, monoclonal


buffered aqueous solution

species reactivity

sheep, horse (IgG), rabbit, goat, human

condiciones de almacenamiento

protect from light


dot immunobinding: 1:16
particle immunofluorescence: 1:16



enviado en

dry ice

temp. de almacenamiento


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Descripción general

Monoclonal Anti-Human IgG (mouse IgG2a isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Immunoglobulins (Igs) belongs immunoglobulin super-family. Each immunoglobin have two heavy (H) and two light (L), held together by disulphide linkages. The light comprises of one variable N-terminal region and a constant C-terminal region. The heavy chain has one variable N-terminal region and three or four constant (CH1-CH4) C-terminal region.


The antibody is specific for the Fc portion of human IgG and recognizes an epitope common to all human IgG subclasses. This antibody was adopted as an Fc specific reagent in the IUIS/WHO study.


Monoclonal Anti-Human IgG (Fc specific)-FITC antibody produced in mouse has been used in:
  • Fluorescent Dot Immunobinding Assay (F-DIBA)
  • Particle Immunofluorescent Assay (F-IFMA)
  • flow cytometry

Acciones bioquímicas o fisiológicas

Digestion of IgG by papain results in generation of fragment antigen binding (Fab) comprising one complete L chain and a variable and CH1 region of H chain. Pepsin digestion of IgG results in fragment crystallisable (fc), containing the H chain constant region. IgG antibody have enormous therapeutic potential and the Fc 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.

Forma física

Solution in 0.01 M phosphate buffer pH 8.0, containing 1% inactivated bovine serum albumin and 15 mM sodium azide.

Cláusula de descargo de responsabilidad

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.


Health hazard

Palabra de señalización


Frases de peligro

Clasificaciones de peligro

Resp. Sens. 1 - Skin Sens. 1

Código de clase de almacenamiento

12 - Non Combustible Liquids



Punto de inflamabilidad F

Not applicable

Punto de inflamabilidad C

Not applicable

Certificado de Análisis

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Certificado de origen

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Quotes and Ordering

Martin Pool et al.
European journal of nuclear medicine and molecular imaging, 44(8), 1328-1336 (2017-03-21)
c-MET and its ligand hepatocyte growth factor are often dysregulated in human cancers. Dynamic changes in c-MET expression occur and might predict drug efficacy or emergence of resistance. Noninvasive visualization of c-MET dynamics could therefore potentially guide c-MET-directed therapies. We
Development and characterization of clinical-grade 89Zr-trastuzumab for HER2/neu immunoPET imaging
Dijkers ECF, et al.
Journal of Nuclear Medicine, 50(6), 974-981 (2009)
Eli C F Dijkers et al.
Journal of nuclear medicine : official publication, Society of Nuclear Medicine, 50(6), 974-981 (2009-05-16)
The anti-human epidermal growth factor receptor 2 (HER2/neu) antibody trastuzumab is administered to patients with HER2/neu-overexpressing breast cancer. Whole-body noninvasive HER2/neu scintigraphy could help to assess and quantify the HER2/neu expression of all lesions, including nonaccessible metastases. The aims of
Jacoba van Zanten et al.
Cancer gene therapy, 11(2), 156-164 (2003-12-27)
In this study, we developed a nonviral, cationic, targeted DNA-carrier system by coupling SAINT/DOPE lipids to monoclonal antibodies. The two monoclonal antibodies used were both tumor specific, that is, MOC31 recognizes the epithelial glycoprotein EGP-2 present in carcinomas and Herceptin
A nonviral carrier for targeted gene delivery to tumor cells
van Zanten J, et al.
Cancer Gene Therapy, 11(2), 156-156 (2004)

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