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Cat. No. | Product Name | Target | Signaling Pathways |
---|---|---|---|
T18997 |
GPDA
Glycylproline p-nitroanilide tosylate,GPN |
Others | Others |
GPDA (Glycylproline p-nitroanilide tosylate) 是一种酶促反应检测底物,用于检测脯氨酰二肽氨基肽酶。 |
Cat. No. | Product Name | Species | Expression System |
---|---|---|---|
TMPY-02120 |
XPNPEP2 Protein, Human, Recombinant (His)
AEACEI,X-prolyl aminopeptidase (aminop... |
Human | HEK293 Cells |
Aminopeptidase P (APP) is a hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. A membrane-bound and soluble form of this enzyme (XPNPEP2) have been identified as products of two separate genes. XPNPEP2, the X-linked gene that encodes membranous aminopeptidase P (APP), has been reported to associate with APP activity. The membrane aminopeptidase P (XPNPEP2) is largely limited in distribution ... | |||
TMPH-00513 |
Proline iminopeptidase Protein, Elizabethkingia meningoseptica, Recombinant (His & Myc)
Proline iminopeptidase,Prolyl aminopeptidase |
Elizabethkingia meningoseptica | E. coli |
Releases the N-terminal proline from various substrates. Cleaves specifically Pro-betaNA and small peptides containing proline at the amino terminal. No activity against hydroxyproline-betaNA. Proline iminopeptidase Protein, Elizabethkingia meningoseptica, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 41.6 kDa and the accession number is O05420. | |||
TMPJ-01351 |
XPNPEP1 Protein, Human, Recombinant (His)
Xaa-Pro Aminopeptidase 1,X-Prolyl Amin... |
Human | E. coli |
X-Prolyl Aminopeptidase (XPNPEP1) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-Prolyl Aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby compleme... |