Aminopeptidase P1 Protein, Human (His-SUMO)

Aminopeptidase P1 Protein, a metalloaminopeptidase, crucially catalyzes the removal of penultimate prolyl residues from peptide N-termini, including substrates like Arg-Pro-Pro. This activity significantly contributes to specific peptide degradation, exemplified in bradykinin processing. Aminopeptidase P1's selective prolyl cleavage underscores its importance in modulating peptide structures and functions within biological systems. Aminopeptidase P1 Protein, Human (His-SUMO) is the recombinant human-derived Aminopeptidase P1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag. The total length of Aminopeptidase P1 Protein, Human (His-SUMO) is 622 a.a., with molecular weight of ~85.8 kDa.

Aminopeptidase P1 Protein, a metalloaminopeptidase, plays a crucial role in peptide metabolism by catalyzing the removal of penultimate prolyl residues from the N-termini of peptides, including substrates such as Arg-Pro-Pro. This enzymatic activity contributes significantly to the degradation of specific peptides, exemplified by its role in the processing of bradykinin. The selective cleavage of prolyl residues by Aminopeptidase P1 underscores its importance in modulating peptide structures and functions within biological systems.

Human

E. coli

N-6*His;N-SUMO

Q9NQW7 (P2-Q623)

7511  [NCBI]

PPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHLLLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSETIPKDHRCCMPYTPICIAKAVKNSAESEGMRRAHIKDAVALCELFNWLEKEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPVPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPVKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDSLTDKECDWLNNYHLTCRDVIGKELQKQGRQEALEWLIRETQPISKQH

Approximately 85.8 kDa

Greater than 90% as determined by SDS-PAGE.