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货号 | bs-3492R-1 |
品牌 | |
浓度 | |
货期 | 现货 |
英文名称 | Rabbit Anti-Phospho-Insulin Receptor Beta (Tyr1355) antibody |
中文名称 | Rabbit Anti-Phospho-Insulin Receptor Beta (Tyr1355) antibody |
产品标签 | 磷酸化抗体 |
研究领域 | 肿瘤,细胞生物,免疫学,细胞凋亡,转录调节因子,激酶和磷酸酶,糖尿病, |
英文别名 | Insulin Receptor (phospho Y1355); Insulin Receptor (phospho Try1355); CD 220; CD220; CD220 antigen; HHF 5; HHF5; HIR B; INSR; INSR; Insulin receptor; Insulin receptor subunit beta; IR; INSR_HUMAN. |
反应物种(已验证) | Human,Mouse,Rat |
产品应用(已验证) | WB,IHC,FCM |
产品应用(可推荐) | IF,ELISA |
推荐稀释比例 | WB=1:500-2000,Elisa=1:5000-10000,IHC-P=1:100-500,IHC-F=1:100-500,Flow Cyt=3ug/Test,IF=1:100-500, |
克隆类型 | 多克隆 |
抗体来源 | Rabbit |
理论分子量 | 68/152 |
细胞定位 | 细胞膜 |
性状 | Liquid |
免疫原 | KLH conjugated Synthesised phosphopeptide derived from human Insulin Receptor alpha around the phosphorylation site of Tyr1355 |
抗原表位 | RS(p-Y)EE |
亚型 | IgG |
纯化方法 | affinity purified by Protein A |
SUBCELLULAR | Membrane; Single-pass type I membrane protein. |
Tissue | Isoform Long and isoform Short are predominantly expressed in tissue targets of insulin metabolic effects: liver, adipose tissue and skeletal muscle but are also expressed in the peripheral nerve, kidney, pulmonary alveoli, pancreatic acini, placenta vasc |
SIMILARITY | Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Contains 3 fibronectin type-III domains. Contains 1 protein kinase domain. |
SUBUNIT | Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain. Forms a hybrid receptor with IGF1R, the hybrid is a tetramer consist |
Function | Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling interme |
Post-translational | After being transported from the endoplasmic reticulum to the Golgi apparatus, the single glycosylated precursor is further glycosylated and then cleaved, followed by its transport to the plasma membrane. Autophosphorylated on tyrosine residues in resp |
DISEASE | Defects in INSR are the cause of Rabson-Mendenhall syndrome (RMS) [MIM:262190]; also known as Mendenhall syndrome. RMS is a severe insulin resistance syndrome characterized by insulin-resistant diabetes mellitus with pineal hyperplasia and somatic abnorma |
SWISS | P06213 |
Gene ID | 3643 |
保存条件 | Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. |
Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
CAS | 3 |
英文介绍 | The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism. Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins. |