PPIL2 Protein, Human, Recombinant (aa 280-457, His Tag)

PPIL2, is an enzyme that belongs to the cyclophilin family. The cyclophilins are peptidylprolyl isomerases and are highly conserved ubiquitous. They play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL2 interacts with the proteinase inhibitor eglin c and is localized in the nucleus. It contains 1 PPIL2 cyclophilin-type domain and 1 U-box domain. PPIL2 accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

At Leading Biology, the biological activity of a recombinant protein is routinely measured using a bioassay, e.g. chemotaxis or cell proliferation assay, enzyme assay, or a functional ELISA. When a recombinant protein is an enzyme, specific activity is derived from an enzymatic assay. Each enzyme is tested for potency by cleavage of a substrate. We are in the process of updating the biological activity data. If you have any questions regarding this update, please feel free to contact our technical support team.

Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. 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 hard copy of CoA.

The recombinant human PPIL2 consists of 193 amino acids and predicts a molecular mass of 21.9 KDa. It migrates as an approximately 24 KDa band in SDS-PAGE under reducing conditions.

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.