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

Uniprot : Q05209

Cat.No.:PKSH031089
Expression host: Baculovirus-Insect Cells

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100μg

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Description

Synonyms	PTP-PEST;PTPG1
Species	Human
Expression_host	Baculovirus-Insect Cells
Sequence	Met 1-Gln355
Accession	AAA36529.1
Mol_Mass	69.4 kDa
AP_Mol_Mass	64 kDa
Tag	N-His-GST
Bio_Activity	Measured by its ability to dephosphorylate a phosphotyrosine residue in an EGF receptor 988-998 phosphopeptide substrate, R&D Systems, Catalog # ES006. The specific activity is > 15 μmoles/min/mg.

Properties

Purity	> 90 % as determined by reducing SDS-PAGE.
Endotoxin level	< 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% Tween80 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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