- $265
- Ybscience
- Yb--0053
- 美国/德国/中国
- 2025年07月13日
- WB
- 详见说明书
- 详见说明书
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- 详细信息
- 文献和实验
- 技术资料
- 抗体名：
VSV-G-tag Antibody
- 抗体英文名：
VSV-G-tag Antibody
- 靶点：
详见说明书
- 浓度：
1.0mg/ml
- 应用范围：
WB
- 宿主：
详见说明书
- 供应商：
上海钰博生物科技有限公司
- 库存：
大量
- 目录编号：
0053
- 抗原来源：
详见说明书
- 保质期：
1年
- 适应物种：
详见说明书
- 标记物：
详见说明书
- 克隆性：
多克隆
- 保存条件：
Store at -20°C
- 形态：
液体或冻干粉
- 亚型：
详见说明书
- 免疫原：
详见说明书
- 规格：
50μg/50μl, 100μg/100μl
-
- Catalog No. : AB0053
- Size : 50μg/50μl, 100μg/100μl
-
- Mol Weight : N/A
- UniProt : N/A
-
- Isotype : Rabbit IgG
- Clonality : Monoclonal
-
- Price : $165/100μg
- Availability : Ship next day
-
- Rank:
- Download datasheet [PDF] :
- Rank:
Category
- Primary Antibodies
- Secondary antibody
- Loading control / tag antibody
Details
Alternative Names:
VSV epitope tag;VSV tag;VSV-G epitope tag;VSVG;vsvg tag
Application:
WB
Reactivity:
All
Dilution:
WB 1:3000~1:10000
 |
Western blot analysis of extracts from VSV-G tag fusion protein, using VSV-G tag antibody. |
Purification:
Affinity-chromatography
Specificity:
VSV-G tag antibody detects endogenous levels of C-terminal, internal, and N-terminal VSV-G-tagged proteins.
Immunogen:
A synthesized peptide
Description:
Vesicular stomatitis virus (VSV), an enveloped RNA virus from the Rhabdoviridae family, is released from the plasma membrane of host cells by a process called budding. The glycoprotein (VSV-g) contains a domain in its extracellular membrane proximal stem that appears to be needed for efficient VSV budding.
Storage Condition and Buffer:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.
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文献和实验Purification and Characterization of His-Tagged Antibody Fragments
, typically His6 , fused to the recombinant protein. In the case of antibody fragments that are composed of different chains, e.g., Fv and Fab, the site of attachment for the His6 tag has to be carefully chosen, and mild chromatographic conditions
Generation of Antibody Molecules Through Antibody Engineering
been overcome to a large extent using genetic-engineering techniques to produce chimeric mouse/human and completely human antibodies. Such an approach is particularly suitable because of the domain structure of the antibody molecule ( 2 ), where functional
The importance of antibody molecules was first recognized in the 1890s, when it was shown that immunity to tetanus and diphtheria was caused by antibodies against the bacterial exotoxins (1 ). Around the same time, it was shown that antisera
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