Previous studies in this laboratory have shown that the SH-2 domaincontaining protein tyrosine phosphatase SHP-1 is expressed in CNS glia and functions to modulate cytokine activities in these cells. The present study demonstrates that SHP-1 is expressed within multiple regions of the CNS in vivo, e
The influence of lysis buffer composition on the expression and activity of protein tyrosine phosphatase
✍ Scribed by Jennifer Calvert-Evers; Kate Hammond
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 93 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0173-0835
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✦ Synopsis
The influence of lysis buffer composition on the expression and activity of protein tyrosine phosphatase Lysis conditions are crucial in the extraction and solubilization of phosphotyrosinecontaining proteins in a form that is immunoreactive, undegraded and enzymatically active. To establish optimal experimental conditions, we evaluated protein tyrosine phosphatase enzyme activity and the detection of PTP-1B protein in human acute promyelocytic leukaemic cells, both before and after retinoic acid treatment. We found that the composition of the lysing buffer greatly influenced the efficiency of solubilization, resulting in major alterations in the activity of protein tyrosine phosphatases and on the mobility of PTP-1B protein.
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