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- 详细信息
- 文献和实验
- 技术资料
- 抗体英文名:
Phospho-Insulin Receptor β (Tyr1361) (84B2) Rabbit mAb
- 抗原:
synthetic phosphopeptide corresponding to residues surrounding Tyr1361 of human insulin receptor β
- 应用范围:
W
- 库存:
大量
- 级别:
详见MSDS文件
- 保质期:
详见说明书
- 供应商:
CST
- 适应物种:
H
- 是否单克隆:
1
- 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
Reactivity Key: H=Human
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) | Isotype |
|---|---|---|---|---|
| W | H | Transfected Only | 95 KDa | Rabbit IgG |
| Protocols |
|
|---|---|
| Specificity / Sensitivity | Phospho-Insulin Receptor β (Tyr1361) (84B2) Rabbit mAb detects transfected levels of insulin receptor β only when phosphorylated at Tyr1361. It slightly cross-reacts with activated IGF-I receptor, but does not cross-react with other activated tyrosine kinases. |
| Source / Purification | Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1361 of human insulin receptor β. Western Blotting
Cross-reactivity testing of Phospho-Insulin Receptor (Tyr1361) (84B2) Rabbit mAb with activated IGF-I receptors. Various amounts of activated recombinant IGF-I receptor cytoplasmic domain proteins were applied for Western blot analysis, using Phospho-Insulin Receptor (Tyr1361) (84B2) Rabbit mAb (upper) and Phospho-IGF-I Receptor (Tyr1315/1316) (19H7) Rabbit mAb #3024 (lower) respectively. The result showed that Phospho-Insulin Receptor (Tyr1361) (84B2) Rabbit mAb barely cross-reacts with activated IGF-I receptors. |
| Background | Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).
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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 |
Rabbit Monoclonals Produced Using Epitomics® Technology, U.S. Patent No. 5,675,063. For Research Use Only. Not For Use In Diagnostic Procedures. |
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文献和实验:使用 Anti-phospho-Akt (Ser473) Rabbit mAb 对石蜡包埋的人乳腺癌组织进行免疫组织化学分析。(图 A)使用免疫组化试剂盒M&R HRP/DAB Detection IHC Kit,抗体 1:100 稀释;(图 B) 采用普通免疫组化试剂盒,抗体 1:25 稀释。 图 6 免疫组化实验检测 Erk1/2 表达 注:使用 Anti-Erk1/2 Mouse mAb与p44/42 MAPK (Erk1/2)Rabbit mAb 对正常小鼠心脏组织进行免疫
Overview of Receptor Allosterism
Figure 1.21.2 Effect of: (A ) negative allosteric modulator, (B ) positive allosteric modulator, or (C ) a competitive antagonist on orthosteric ligand‐receptor occupancy (ρA ). For all the simulations, p K
B-Cell Signal Transduction: Tyrosine Phosphorylation, Kinase Activity, and Calcium Mobilization
Signal transduction by the B-cell antigen receptor (BCR) regulates development, survival, and clonal expansion of B cells. The BCR complex comprises the membrane-bound immunoglobulin molecule and the Ig-α/Ig-β heterodimer, and was shown to form
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