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. The total length of PPIase A Protein, E.coli (His-SUMO) is 166 a.a., with molecular weight of ~34.1 kDa.

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.

E.coli

E. coli

N-His;N-SUMO

P0AFL5 (25A-190P)

66672756  [NCBI]

AKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAKVLP

Approximately 34.1 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.