PPIase A Protein, E.coli (His-SUMO)
The PPIase A protein plays a central role in complex protein folding, utilizing its peptidyl-prolyl cis-trans isomerase (PPIase) activity to accelerate dynamic conformational changes that are critical for proper protein maturation. PPIase A specifically catalyzes the cis-trans isomerization of proline imide peptide bonds, effectively promoting protein folding. PPIase A Protein, E.coli (His-SUMO) is the recombinant E. coli-derived PPIase A protein, expressed by E. coli , with N-His, N-SUMO labeled tag.
- Species: E.coli
- Source: E. coli
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
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Biological Activity
Description
The PPIase A protein plays a central role in complex protein folding, utilizing its peptidyl-prolyl cis-trans isomerase (PPIase) activity to accelerate dynamic conformational changes that are critical for proper protein maturation. PPIase A specifically catalyzes the cis-trans isomerization of proline imide peptide bonds, effectively promoting protein folding. PPIase A Protein, E.coli (His-SUMO) is the recombinant E. coli-derived PPIase A protein, expressed by E. coli , with N-His, N-SUMO labeled tag.
Background
PPIase A Protein emerges as a key player in the intricate process of protein folding, leveraging its peptidyl-prolyl cis-trans isomerase (PPIase) activity to accelerate the dynamic conformational changes crucial for proper protein maturation. With a specific role in catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides, PPIase A facilitates the efficient folding of proteins. This enzymatic capability underscores its significance in maintaining the structural integrity of nascent or misfolded polypeptides, contributing to the overall cellular protein homeostasis. The multifunctional role of PPIase A in orchestrating protein folding processes positions it as a key molecular player in cellular physiology, prompting further exploration to elucidate the specific molecular mechanisms and cellular contexts through which PPIase A actively contributes to the intricate choreography of protein folding.
Technical Parameters
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Species E.coli
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Source E. coli
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Tag N-His;N-SUMO
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Accession
P0AFL5 (A25-P190)
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Gene ID66672756 [NCBI]
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Molecular Construction
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N-term
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6*His-SUMO
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PPIase A (A25-P190)
Accession # P0AFL5 -
C-term
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Protein Length
Full Length of Mature Protein
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Synonyms
PPIA; Epididymis Secretory Sperm Binding Protein Li 69p; Peptidylprolyl Isomerase A; Peptidylprolyl Isomerase A (Cyclophilin A); CYPA; Peptidyl-Prolyl Cis-Trans Isomerase; Peptidyl-Prolyl Cis-Trans Isomerase A; T Cell Cyclophilin; Cyclosporin A-Binding Pr
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AA Sequence
AKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAKVLP
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Predicted Molecular Mass
34.1 kDa
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Purity
≥ 90%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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