| Short Description : | Recombinant-Human FKBP13/FKBP2-No-Tag protein was developed from e.coli and has a target region of No-Tag. For use in research applications. |
| Applications: | SDS-PAGE/Enzyme Activity |
| Host: | E.coli |
| Note: | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Concentration: | 1 mg/mL |
| Formulation: | Liquid in 20mM Tris-HCl buffer (pH 8.0) containing 10% Glycerol, 1mM DTT |
| Storage Instruction: | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
| Endotoxin: | < 1 EU per 1ug of protein (determined by LAL method) |
| Immunoreactivity: | Specific activity is > 700nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmol of suc-AAPF-pNA per minute at 37C in Tris-HCl pH 8.0 using chymotrypsin. |
| Gene Symbol: | FKBP2 |
| Gene ID: | 2286 |
| Uniprot ID: | FKBP2_HUMAN |
| Accession Number: | NP_001128680 |
| Immunogen: | Human |
| Immunogen Region: | 22-142aa |
| Immunogen Sequence: | MATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK IPGGATLVFE VELLKIERRT EL |
| Tissue Specificity | T-cells and thymus. |
| Function | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
| Protein Name | Peptidyl-Prolyl Cis-Trans Isomerase Fkbp2Ppiase Fkbp213 Kda Fk506-Binding Protein13 Kda FkbpFkbp-13Fk506-Binding Protein 2Fkbp-2Immunophilin Fkbp13Rotamase |
| Database Links | |
| Cellular Localisation | Endoplasmic Reticulum MembranePeripheral Membrane Protein |
| Alternative Protein Names | Peptidyl-Prolyl Cis-Trans Isomerase Fkbp2 proteinPpiase Fkbp2 protein13 Kda Fk506-Binding Protein protein13 Kda Fkbp proteinFkbp-13 proteinFk506-Binding Protein 2 proteinFkbp-2 proteinImmunophilin Fkbp13 proteinRotamase proteinFKBP2 proteinFKBP13 protein |
Information sourced from Uniprot.org

