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| Product | Description | |
|---|---|---|
| peptidylprolyl isomerase | The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. Group: Enzymes. Synonyms: PPIase; cyclophilin [misleading, see comments]; peptide bond isomerase; peptidyl-prolyl cis-trans isomerase. Enzyme Commission Number: EC 5.2.1.8. CAS No. 95076-93-0. Peptidylprolyl Isomerase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5450; peptidylprolyl isomerase; EC 5.2.1.8; 95076-93-0; PPIase; cyclophilin [misleading, see comments]; peptide bond isomerase; peptidyl-prolyl cis-trans isomerase. Cat No: EXWM-5450. |  |
| Peptidylprolyl Isomerase F (PPIF) Recombinant, Mouse, Unstained Protein Molecular Weight Marker | Peptidylprolyl Isomerase F (PPIF) Recombinant, Mouse, Unstained Protein Molecular Weight Marker. Group: Molecular Biology. Grades: Highly Purified. Pack Sizes: 15ul. US Biological Life Sciences. |  Worldwide |
| Cyclophilin A from Human, Recombinant | Cyclophilins are peptidyl prolyl isomerases that catalyze the cis-trans isomerization of X-Pro peptide bonds. They are highly-conserved cytoplasmic enzymes that accelerate protein folding and facilitate HIV infectivity. Cyclosporin A binds to cyclophilin and inhibits its activity. The cyclosporin A-cyclophilin complex binds to calcineurin and inhibits T-cell activation. The structure of human, recombinant cyclophilin is given by Holzman, et al. Group: Enzymes. Synonyms: PPIase; cyclophilin; peptide bond isomerase; peptidyl-prolyl cis-trans isomerase; peptidylprolyl isomerase; EC 5.2.1.8; 95076-93-0; PPIA; CYPA; CYPH; HEL-S-69p. Enzyme Commission Number: EC 5.2.1.8. CAS No. 95076-93-0. Purity: >95% (SDS-PAGE). Peptidylprolyl Isomerase. Storage: Store at -20°C. Form: Buffered aqueous solution. Source: E. coli. Species: Human. PPIase; cyclophilin; peptide bond isomerase; peptidyl-prolyl cis-trans isomerase; peptidylprolyl isomerase; EC 5.2.1.8; 95076-93-0; PPIA; CYPA; CYPH; HEL-S-69p. Cat No: NATE-0823. | |
| Peptidyl-Prolyl Cis/Trans Isomerase from Human, Recombinant | Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor...ase Pin1; DOD; UBL5; PIN1; PPIase. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. Peptidylprolyl Isomerase. Mole weight: 18.2 kDa. Activity: > 162 nmoles/min/ug. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. Species: Human. Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; EC 5.2.1.8; Rotamase Pin1; PPIase Pin1; DOD; UBL5; PIN1; PPIase. Cat No: NATE-0910. | |
| Suc-Ala-Glu-Pro-Phe-pNA | Suc-AEPF-pNA can be used as a chromogenic substrate for the peptidylprolyl isomerase Pin1. Synonyms: Suc-AEPF-pNA. Grades: ≥ 99%. CAS No. 128802-76-6. Molecular formula: C32H38N6O11. Mole weight: 682.69. |  |
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