- 询价
- Signalway Antibody
- 48389
- 2025年09月23日
- WB, ICC, FC
- Mouse
- Human;Mouse
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- 详细信息
- 文献和实验
- 技术资料
- 免疫原：
Recombinant protein
- 形态：
liquid
- 保存条件：
Store at -20˚C
- 克隆性：
Monoclonal
- 适应物种：
Human;Mouse
- 保质期：
12 months
- 抗原来源：
Mouse
- 供应商：
南京赛戈巍生物科技有限公司
- 宿主：
Mouse
- 应用范围：
WB, ICC, FC
- 靶点：
Uniprot：P29353
- 抗体英文名：
SHC1 Antibody
- 规格：
50ul/100ul
p66 antibody
p66SHC antibody
SH2 domain protein C1 antibody
SHC (Src homology 2 domain containing) transforming protein 1 antibody
SHC 1 antibody
SHC A antibody
SHC adaptor protein 1 antibody
Shc antibody
SHC transforming protein 1 antibody
SHC transforming protein antibody
SHC-transforming protein 1 antibody
SHC-transforming protein 3 antibody
SHC-transforming protein A antibody
SHC1 antibody
SHC1_HUMAN antibody
SHCA antibody
Src homology 2 domain-containing-transforming protein C1 antibody
计算分子量:63 kDa
配方:1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.
应用详情:WB: 1:500-1:2,000
IHC: 1:50-1:200
ICC: 1:50-1:200
FC: 1:50-1:100
图片:
Western blot analysis of SHC1 on?human SHC1 recombinant protein using anti-SHC1 antibody at 1/1,000 dilution.
,
Western blot analysis of SHC1 on HEK293 (1) and SHC1-hIgGFc transfected HEK293 (2) cell lysate using anti-SHC1 antibody at 1/1,000 dilution.
,
Western blot analysis of SHC1 on NIH/3T3?cell lysate using anti-SHC1 antibody at 1/1,000 dilution.
,
ICC staining SHC1 (green) and Actin filaments (red) in A431 cells. The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
,
Flow cytometric analysis of NIH/3T3?cells with SHC1 antibody at 1/100 dilution (green) compared with an unlabelled control (cells without incubation with primary antibody; red).
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文献和实验Monitoring Nutrient Signaling Through the Longevity Protein p66SHC1
to nutrients through the longevity protein p66SHC1 and the mTOR/S6K cascade, which might be used to study cellular senescence and its chemical modulation by pharmaceutical agents in vitro.
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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