Overview |
bs-70133r-100ul |
Insulin Receptor (Thr1160) Antibody |
WB |
Specific for endogenous levels of the ~95 kDa Insulin receptor phosphorylated at Thr1160. Immunolabeling is completely eliminated with λ-phosphatase treatment. |
Human |
Mouse, Rat, Dog, Bovine, Xenopus, Non-Human Primate |
Specifications |
Unconjugated |
Rabbit |
Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr1160 of human insulin receptor, conjugated to keyhole limpet hemocyanin (KLH). |
Thr1160 |
Polyclonal |
IgG |
Lot Dependent |
Antigen Affinity purification from Pooled whole antiserum |
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol. |
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. |
Target |
3643 |
P06213 |
CD220 antibody, HHF5 antibody, human insulin receptor antibody, Insr antibody, INSR_HUMAN antibody, Insulin receptor subunit beta antibody, IR 1 antibody, IR antibody, IR-1 antibody, IR1 antibody, |
The insulin receptor (IR) is a well-studied receptor tyrosine kinase composed of two α subunits, responsible for the extracellular insulin binding site, and two β subunits, responsible for intracellular protein kinase activity (Endemann et al., 1990, Chiu et al., 2010). The binding of insulin to the α subunits activates the intrinsic kinase activity located in the β subunits and subsequently initiates a cascade of phosphorylation events causing major conformational changes in the activation loop of the kinase domain, which lead to different biological functions (Chiu et al., 2010). It has been hypothesized that Thr-1160 phosphorylation affects or is affected by Tyr-1158/62/63 phosphorylation and that the conformation of Thr-1160 and pThr-1160 is likely to be affected by the phosphorylation status of the surrounding tyrosines. |
Application Dilution |
WB |
1:300-5000 |