Recombinant Human PTPN12 Protein (aa 1-355, His & GST Tag)(Active) | PKSH031089

Recombinant Human PTPN12 Protein (aa 1-355, His & GST Tag)(Active) | PKSH031089 | Gentaur US, UK & Europe Disrtribition

Synonyms: PTP-PEST;PTPG1

Active Protein: Active protein

Activity: A DNA sequence encoding the human PTPN12 (AAA36529.1) (Met1-Gln355) was expressed with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Protein Construction: A DNA sequence encoding the human PTPN12 (AAA36529.1) (Met1-Gln355) was expressed with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Fusion Tag: N-His & GST

Species: Human

Expressed Host: Baculovirus-Insect Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and 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.

Molecular Mass: 69.4 kDa

Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% gly, pH 8.0

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.

Research Area: N/A