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Merck
CN

F5016

Sigma-Aldrich

抗-人IgG(Fc特异性)单克隆抗体

clone HP-6017, purified from hybridoma cell culture

别名:

Monoclonal Anti-Human IgG (Fc specific)

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UNSPSC代码:
12352203
NACRES:
NA.46
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生物来源

mouse

偶联物

FITC conjugate

抗体形式

purified from hybridoma cell culture

抗体产品类型

secondary antibodies

克隆

HP-6017, monoclonal

表单

buffered aqueous solution

种属反应性

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

储存条件

protect from light

技术

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

同位素/亚型

IgG2a

运输

dry ice

储存温度

−20°C

靶向翻译后修饰

unmodified

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一般描述

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.

应用

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

生化/生理作用

该抗体对人 IgG 的 Fc 部分具有特异性,并识别所有人 IgG 亚类共有的表位。在 IUIS/WHO 研究中,该抗体被用作 Fc 特异性试剂。
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.

外形

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

免责声明

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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象形图

Health hazard

警示用语:

Danger

危险声明

危险分类

Resp. Sens. 1 - Skin Sens. 1

储存分类代码

12 - Non Combustible Liquids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品
含少量动物源组分生物产品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Minwoo Kang et al.
Pharmaceutics, 14(7) (2022-07-28)
Immuno-positron emission tomography (PET) has great potential to evaluate the target expression level and therapeutic response for targeted cancer therapy. Immuno-PET imaging with pertuzumab, due to specific recognition in different binding sites of HER2, could be useful for the determination
A nonviral carrier for targeted gene delivery to tumor cells
van Zanten J, et al.
Cancer Gene Therapy, 11(2), 156-156 (2004)
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
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
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)

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