
Thermo Fisher Scientific Phospho-PTPRA (Tyr798) Polyclonal Antibody
Phospho-PTPRA (Tyr798)에 특이적인 Thermo Fisher Scientific의 rabbit polyclonal antibody. WB, IHC, ICC, ELISA 등 다양한 응용에 적합. Protein A로 정제된 고순도 항체로 안정적인 액상 형태 제공. 연구용으로만 사용 가능.
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Applications and Tested Dilution
| Application | Tested Dilution |
|---|---|
| Western Blot (WB) | 1:500–1:2,000 |
| Immunohistochemistry (Paraffin) (IHC (P)) | 1:100–1:500 |
| Immunohistochemistry (Frozen) (IHC (F)) | 1:100–1:500 |
| Immunocytochemistry (ICC/IF) | 1:50–1:200 |
| ELISA | 1:500–1:1,000 |
Product Specifications
| Specification | Description |
|---|---|
| Species Reactivity | Human, Mouse, Rat |
| Host / Isotype | Rabbit / IgG |
| Class | Polyclonal |
| Type | Antibody |
| Immunogen | KLH conjugated synthetic phosphopeptide derived from human PTPRA around the phosphorylation site of Tyr798 |
| Conjugate | Unconjugated |
| Form | Liquid |
| Concentration | 1 mg/mL |
| Purification | Protein A |
| Storage Buffer | 0.01M TBS, pH 7.4, with 1% BSA, 50% glycerol |
| Contains | 0.02% ProClin 300 |
| Storage Conditions | -20°C |
| Shipping Conditions | Ambient (domestic); Wet ice (international) |
Target Information
Phosphorylation of receptors by protein kinases is a process that can be reversed by a group of enzymes called protein phosphatases. Coordinated control of kinases and phosphatases provides the cell with the capacity to rapidly switch between phosphorylated and dephosphorylated protein states in dynamic response to environmental stimuli. Activation of critical enzymes by kinase phosphorylation alone is not enough to provide adequate regulation — it is the combination with phosphatase dephosphorylation that effectively creates on/off switches to control cellular events.
Errors in control, either through kinases or their counterpart phosphatases, can lead to unchecked cell growth attributable to human cancers and developmental disorders. Potential mechanisms to control dephosphorylation include changes in the expression of protein phosphatases, their subcellular localization, phosphorylation of phosphatase catalytic and regulatory subunits, and regulation by endogenous phosphatase inhibitors.
Most protein phosphatases are not stringently specific for their substrates. Consequently, changes in phosphatase activity may have a broad impact on dephosphorylation and turnover of phosphoproteins that are substrates for different kinases. This may be an important point of control to connect cellular circuitry of interrelated signaling pathways and to synchronize physiological responses.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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