- 询价
- Cell Signaling Technology
- 9552
- USA
- 2025年09月02日
- W, IP
- Rabbit
- H,M,R,Hm,Mk,C
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- 详细信息
- 文献和实验
- 技术资料
- 抗体英文名：
PTEN Antibody
- 抗原：
synthetic peptide corresponding to the carboxy terminus of human PTEN
- 应用范围：
W, IP
- 宿主：
Rabbit
- 供应商：
CST
- 级别：
详见MSDS文件
- 保质期：
详见说明书
- 库存：
大量
- 适应物种：
H,M,R,Hm,Mk,C
- 是否单克隆：
2
- 保存条件：
-20°c
- 规格：
100 ul (10 western blots)/carrier free & custom formulation / quantity
| 规格： | 产品价格： | ￥请询价 | |
|---|---|---|---|
| 规格： | 100 ul (10 western blots) | 产品价格： | ￥请询价 |
| 规格： | carrier free & custom formulation / quantity | 产品价格： | ￥请询价 |
pathway more info application references datasheet PDF MSDS PDF protocols
Applications Key: W=Western Blotting IP=Immunoprecipitation
Reactivity Key: H=Human M=Mouse R=Rat Hm=Hamster Mk=Monkey C=Chicken
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IP | H M R Hm Mk (C) | Endogenous | 54 | Rabbit |
| Protocols |
|
|---|---|
| Specificity / Sensitivity | PTEN Antibody detects endogenous levels of total PTEN protein. The antibody does not cross-react with related proteins. |
| Source / Purification | Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of human PTEN. Antibodies are purified by protein A and peptide affinity chromatography. Western Blotting
Western blot analysis of extracts from HeLa cells, transfected with 100 nM SignalSilence® Control siRNA (Fluorescein Conjugate) #6201 (-) or SignalSilence® PTEN siRNA I (+), using PTEN Antibody #9552 and p42 MAPK (Erk2) Antibody #9108. PTEN Antibody confirms silencing of PTEN expression, while the p42 MAPK (Erk2) Antibody is used to control for loading and specificity of PTEN siRNA. Western Blotting
Western blot analysis of extracts from HeLa cells, transfected with 100 nM SignalSilence® Control siRNA (Fluorescein Conjugate) #6201 (-) or SignalSilence® PTEN siRNA II (+), using PTEN (138G6) Rabbit mAb and β-Actin (13E5) Rabbit mAb #4970. PTEN (138G6) Rabbit mAb confirms silencing of PTEN expression, while the β-Actin (13E5) Rabbit mAb is used to control for loading and specificity of PTEN siRNA Western Blotting
Western blot analysis of extracts from various cell lines, using PTEN Antibody. |
| Background | PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).
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| Application References |
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know ! |
| Companion Products |
For Research Use Only. Not For Use In Diagnostic Procedures. |
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文献和实验Genetic evidence strongly suggested that a tumor suppressor was located on chromosome 10. During the development of glioblastoma, one copy of chromosome 10 was typically lost (1 ). Cytogenetic and molecular analysis revealed partial
Measurement of PTEN Activity in vivo by Imaging Phosphorylated Akt
-dependent activation and phosphorylation of the survival kinase Akt can be used as readout for cellular PTEN activity. Here we have outlined a detailed procedure employing a phosphoserine-specific anti-Akt antibody to examine the content of phosphorylated
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
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