Analytical Data
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Gene name
CYPB
- Application
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Alternative Names
CYPB；CYPB；Peptidyl-prolyl cis-trans isomerase B
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23284
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Expression Region
34-216aa
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AA Sequence
MKHHHHHHASDEKKKGPKVTVKVYFDLRIGDEDVGRVIFGLFGKTVPKTV DNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERF PDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVL EGMEVVRKVESTKTDSRDKPLKDVIIADCGKIEVEKPFAIAKE
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Molecular Weight
22 kDa
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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
Related Products
Protein Description
CYPB, or Cyclophilin B, is a member of the cyclophilin family of proteins known for their peptidyl-prolyl isomerase activity, which plays a crucial role in protein folding and cellular signaling. The study of CYPB has gained prominence due to its involvement in various biological processes, including immunoregulation, viral replication, and stress response. Research has indicated that CYPB is implicated in several diseases, including cancer and neurodegenerative disorders. Its role as a chaperone in the endoplasmic reticulum suggests potential therapeutic applications, particularly in the enhancement of protein folding and stability. Additionally, CYPB has been linked to the modulation of immune responses, making it a target for investigating novel immune therapies. Recent studies have focused on recombinant protein technology to produce CYPB for structural and functional analyses, aiming to elucidate its mechanisms of action and interactions with other biomolecules. Understanding the properties and functions of CYPB through recombinant approaches may provide insights into its potential as a biomarker or therapeutic target and could pave the way for developing new strategies to combat related diseases. Overall, the ongoing research on CYPB underscores its significance in biotechnology and medical research, with promising possibilities for clinical applications.
