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Anti-Insulin Receptor (Thr1160) Antibody
Our Anti-Insulin Receptor (Thr1160) rabbit polyclonal phosphospecific primary antibody from PhosphoS
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P06213 |
|---|---|
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 156333 Da |
| Gene ID | 3643 |
|---|---|
| Other Names | 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, |
| Target/Specificity | 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. |
| Format | Antigen Affinity Purified from Pooled Serum |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Anti-Insulin Receptor (Thr1160) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
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