- 询价
- Cell Signaling Technology
- 9339
- USA
- 2025年10月18日
- W, IP
- Rabbit
- H,M,R
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- 详细信息
- 文献和实验
- 技术资料
- 抗体英文名：
Phospho-TAK1 (Ser412) Antibody
- 抗原：
synthetic phosphopeptide corresponding to residues surrounding serine 412
- 应用范围：
W, IP
- 宿主：
Rabbit
- 适应物种：
H,M,R
- 保质期：
详见说明书
- 库存：
大量
- 级别：
详见MSDS文件
- 供应商：
CST
- 是否单克隆：
2
- 保存条件：
-20°c
- 规格：
100 ul (10 western blots)/300 ul (30 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： | 300 ul (30 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
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 | Endogenous | 78 | Rabbit |
| Protocols |
|
|---|---|
| Specificity / Sensitivity | Phospho-TAK1 (Ser412) Antibody detects endogenous levels of TAK1 only when phosphorylated at serine 412. |
| Source / Purification | Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding serine 412. Antibodies are purified by protein A and peptide affinity chromatography. Western Blotting
Western blot analysis of extracts from K562 cells treated with or without lambda phosphatase, using Phospho-TAK1 (Ser412) Antibody #9339 (left) or TAK1 Antibody #4505 (right). Western Blotting
Western blot analysis of extracts from K562 (human), C2C12 (mouse) and C6 (rat) cell lines, using Phospho-TAK1 (Ser412) Antibody. |
| Background | TAK1 is a mitogen-activated protein kinase kinase kinase that can be activated by TGF-β, bone morphogenetic protein and other cytokines including IL-1 (1,2). In vivo activation of TAK1 requires association with TAK1 binding protein 1 (TAB1), which triggers phosphorylation of TAK1 (3,4). Another adaptor protein, TAB2, links TAK1 with TRAF6 and mediates TAK1 activation upon IL-1 stimulation (5). Once activated, TAK1 phosphorylates MAPK kinases MKK4 and MKK3/6, which activate p38 MAPK and JNK, respectively. In addition, TAK1 activates the NF-κB pathway by interacting with TRAF6 and phosphorylating the NF-κB inducing kinase (NIK) (2). TAK1 activation requires multiple phosphorylations in its activation loop. Mutations at Thr187 and Thr184, residues located in the activation loop of TAK1, impairs phosphorylation of both TAK1 and TAB1 and reduces the kinase activity of TAK1, suggesting that autophosphorylation of these residues is necessary for TAK1 activation (4). TAK1 is also phosphorylated at Ser412 in a PKA-dependent manner (6). A mutation of Ser412 to alanine acts as a dominant negative for PKA-enhanced degradation of IκBα, phosphorylation of p38 MAPK and prostaglandin E2-enhances osteoclastic differentiation in RAW264.7 cells (6).
|
| 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Cell Metab：西京医院王琳教授团队报道非酒精性脂肪肝炎新靶点
Metabolism 上在线发表了题为 Tripartite motif 16 ameliorates nonalcoholic steatohepatitis by promoting the degradation of phospho-TAK1 的研究成果 (4)。该研究发现 E3 泛素连接酶 TRIM16 通过促进 p-TAK1 的泛素化依赖性降解，改善 NASH 进展过程中的脂质积累和炎症。 图片来源：Cell Metabolism研究内容肝细胞的脂肪毒性诱导 TRIM16 的表达脂肪毒性是脂质过度积累
Using Phospho‐Motif Antibodies to Determine Kinase Substrates
comprising both the phosphorylated residue and the surrounding residues that determine kinase specificity, with degenerate residues taking up the remaining positions. Currently, several categories of phospho?motif antibody are commercially available
Optimized Protocol to Make Phospho-Specific Antibodies that Work
, not simply its level of expression. In this review, we will discuss both the design of the phosphopeptide immunogen and immunization. The affinity purification of the phospho-specific antibody as well as the methods most suitable for characterizing
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