|Tested species reactivity||Human|
|Host / Isotype||Mouse / IgG1|
|Immunogen||Recombinant human protein purified from E.coli|
|Purification||Ammonium sulfate precipitation|
|Storage buffer||HEPES with 0.15M NaCl, 0.01% BSA, 50% glycerol|
|Contains||0.03% sodium azide|
|Tested Applications||Dilution *|
|Immunoprecipitation (IP)||1 ul|
|Western Blot (WB)||1:2000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
A suggested positive control for this product is HepG2 cells.
Protein tyrosine phosphatases (PTPs) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Together with tyrosine kinases, PTPs regulate the phosphorylation state of many important signaling molecules, such as the MAP kinase family. Recently, increasing attention has been focused on the growing family of PTPs. Like PTKs, PTPs have been implicated in cell signaling, cell growth and proliferation, and oncogenic transformation. Moreover, some PTPs can be involved in cell cycle regulation and embryogenesis. Dual specificity phosphatases (DSPs) are an emerging subclass of the protein tyrosine phosphatase (PTP) gene superfamily, which appears to be selective for dephosphorylating the critical phosphothreonine and phosphotyrosine residues. The prototypical DSP is the VH1 gene in vaccinia virus expressed in late-stage viral infection. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.