Analytical Data
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Gene name
Cyclophilin B/PPIB
- Application
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Alternative Names
PPIB; PPI-B; CYP-S1; CyP-B; SCYLP; PPIase B; Rotamase B; S-cyclophilin; Peptidylprolyl Isomerase B; Peptidyl-Prolyl Cis-Trans Isomerase B
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P23284
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Expression Region
Tyr47~Glu216
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Molecular Weight
20kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Cyclophilin B (CypB), encoded by the PPIB gene, is a peptidyl-prolyl cis-trans isomerase that plays a critical role in protein folding and cellular processes, such as signal transduction and immune response. Its involvement in several physiological and pathological conditions, including viral infections, cancer, and neurodegenerative diseases, has garnered significant research interest. Specifically, CypB has been identified as a crucial factor in HIV replication and is known to interact with viral proteins. The ability to produce recombinant CypB has advanced our understanding of its biological functions and interactions. By utilizing techniques such as recombinant DNA technology and mammalian expression systems, researchers can generate large quantities of CypB for structural and functional studies. These investigations have provided insights into the enzyme's catalytic mechanisms, its role in chaperoning proteins, and its potential as a therapeutic target. Moreover, recombinant CypB is used in drug screening assays and therapeutic interventions aimed at modulating its activity, which could lead to novel treatments for diseases associated with CypB dysfunction. Thus, the study of recombinant CypB remains a significant focus in molecular biology and pharmacology, promising advancements in medical applications through a deeper understanding of this versatile protein.
