Recombinant Human PTPN12 Protein (PKSH031088)
For research use only.
| Synonyms | PTP-PEST, PTPG1 |
| Species | Human |
| Expression Host | Baculovirus-Insect Cells |
| Sequence | Met 1-Gln355 |
| Accession | AAA36529.1 |
| Calculated Molecular Weight | 41.8 kDa |
| Observed Molecular Weight | 41 kDa |
| Tag | None |
| Bio-activity | Measured by its ability to dephosphorylate a tyrosine residue in a peptide containing the EGFR Y992 phosphorylation site. The specific activity is > 20µmol/min/mg |
| Purity | > 85 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation |
Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 8.0 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
| Background | PTPN12 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTPN12 contains a C-terminal PEST motif, which serves as a protein–protein interaction domain, and may be related to protein intracellular half-life. PTPN12 was found to bind and dephosphorylate the product of oncogene c-ABL, thus may play a role in oncogenesis. PTPN12 was shown to interact with, and dephosphorylate, various of cytoskeleton and cell adhesion molecules, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and paxillin, which suggested its regulatory roles in controlling cell shape and mobilit. |
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