Human PTPN12 recombinant protein

Human PTPN12 recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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.

Tyrosine-protein phosphatase non-receptor type 12

MPTP-PEST; PTP-P19; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 12; PTPG1; TCAG7.1075; NON-RECEPTOR TYPE 12; PROTEIN-TYROSINE PHOSPHATASE P19; PROTEIN TYROSINE PHOSPHATASE; PTP-PEST; P19-PTP; PROTEIN-TYROSINE PHOSPHATASE G1; PTPN12; NON-RECEPTOR TYPE 12

Q05209

PTPN12

Baculovirus-Insect Cells

A DNA sequence encoding the human PTPN12 (AAA36529.1) (Met1-Gln355) was expressed and purified with two additional amino acids (Gly & Pro) at the N-terminus.

Human

The secreted recombinant human PTPN12 consists of 357 amino acids and predicts a molecular mass of 41.8 KDa. The apparent molecular mass of the protein is approximately 41 KDa in SDS-PAGE under reducing conditions due to glycosylation.

> 85 % as determined by SDS-PAGE

Measured by its ability to dephosphorylate a tyrosine residue in a peptide containing the EGFR Y992 phosphorylation site (Catalog # ES006).
The specific activity is >20 µmol/min/mg.