PPIase / FKBP7 Protein

Produkt-Information von PPIase / FKBP7 Protein

QC Testing von PPIase / FKBP7 Protein

Purity	> 90 % as determined by SDS-PAGE	SDS-PAGE: PPIase protein
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	Gln 24
Molecular Mass	The recombinant human FKBP7/Fc is a disulfide-linked homodimer. The reduced monomer comprises 436 amino acids and has a predicted molecular mass of 49.4 kDa. The apparent molecular mass of the protein is approximately 55kDa in SDS-PAGE under reducing conditions.
Formulation	Lyophilized from a 0.2μm filtered solution of PBS, pH7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

Usage Guide von PPIase / FKBP7 Protein

Verwandte Produkte & Themen von PPIase / FKBP7 Protein

Enzyme>>Phosphatase & Regulator>>PPIase

Signal Transduction>>Phosphatase & Regulator>>PPIase

Beschreibung von PPIase / FKBP7 Protein

PPIases contains 1 PPIase cyclophilin-type domain and belongs to the cyclophilin-type PPIase family, PPIL3 subfamily. It also is a member of the immunophilin protein family. Members of this family play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. It also may be involved in pre-mRNA splicing.PPIases has a very high substrate specificity for the four-residue peptide Ala-Ala-Pro-Phe only when the proline peptide bond is in the trans state. It is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It interacts with several intracellular signal transduction proteins including type I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels, and coordinates multi-protein complex formation of the tetrameric skeletal muscle ryanodine receptor.

References

1. Shor B. et al., 2008, Cancer Res. 68(8):2934-43.
2. Talmud PJ. et al., 2009, Am J Hum Genet. 2009 Nov;85(5):628-42.
3. Deleersnijder A. et al., 2011, J Biol Chem. 286(30):26687-701.

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