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- 详细信息
- 文献和实验
- 技术资料
- 免疫原:
Recombinant protein encompassing a sequence within the center region of human ASL. The exact sequence is proprietary.
- 亚型:
IgG
- 形态:
Liquid
- 保存条件:
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
- 克隆性:
Polyclonal
- 标记物:
Unconjugated
- 适应物种:
Human
- 保质期:
12 months from the shipping date of the product.
- 抗原来源:
Human
- 目录编号:
GTX109750
- 级别:
Primary Antibodies
- 库存:
Available
- 供应商:
GeneTex
- 宿主:
Rabbit
- 应用范围:
WB, ICC/IF, IHC-P
- 浓度:
1 mg/ml (Please refer to the vial label for the specific concentration.)
- 靶点:
ASL
- 抗体英文名:
ASL antibody
- 抗体名:
ASL 抗体
- 规格:
100 μl/25 μl
| 规格: | 100 μl | 产品价格: | ¥4000.0 |
|---|---|---|---|
| 规格: | 25 μl | 产品价格: | ¥1700.0 |
Wild-type (WT) and ASL knockout (KO) HeLa cell extracts (30 μg) were separated by 10% SDS-PAGE, and the membrane was blotted with ASL antibody (GTX109750) diluted at 1:1000. The HRP-conjugated anti-rabbit IgG antibody (GTX213110-01) was used to detect the primary antibody.
ASL antibody detects ASL protein at cytoplasm and nucleus by immunofluorescent analysis.
Sample: HeLa cells were fixed in 4% PFA at RT for 15 min.
Green: ASL protein stained by ASL antibody (GTX109750) diluted at 1:500.
Blue: Hoechst 33342 staining.
Sample (30 ug of whole cell lysate)
A: MOLT4 (GTX27912)
10% SDS PAGE
GTX109750 diluted at 1:1000
Immunohistochemical analysis of paraffin-embedded DLD1 xenograft, using ASL(GTX109750) antibody at 1:500 dilution.
Antigen Retrieval: Trilogy™ (EDTA based, pH 8.0) buffer, 15min
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文献和实验Methods for ASL Measurements and Mucus Transport Rates in Cell Cultures
The healthy human respiratory tract is lined with a pseudostratified epithelia composed of ∼80% ciliated cells and ∼20% goblet cells. These cells produce and are bathed by a layer of airway surface liquid (ASL), which plays a critical role
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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