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Three different forms of human pancreatic procarboxypeptidase A have been isolated. Additionally we are shipping Carboxypeptidase A4 Proteins (9) and Carboxypeptidase A4 Kits (8) and many more products for this protein.
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Knockdown of cpa6 mRNA also reduced levels of mRNAs encoding neuropeptide precursors (bdnf, npy, chga, pcsk1nl, tac1, nts, edn1), a neuropeptide processing enzyme (cpe), transcription factor (c-fos), and molecules implicated in glutamatergic signaling
CPA4 functions in neuropeptide processing and regulation in the extracellular environment
The crystal structure of the human CPA4 carboxypeptidase in complex with SmCI, a peptide protease inhibitor.
NvCL form Nerita versicolor is a tight-binding inhibitor that interacts with the active site of the CPA4 in a substrate-like manner.
CPA4 gene is imprinted, with preferential expression from the maternal allele in many fetal tissues, but not in fetal brain.
The three-dimensional structure of procarboxypeptidase-A4 (hPCPA4) has been solved and shows the features of related metallocarboxypeptidase zymogens, with a preformed alpha/beta/-hydrolase active-enzyme moiety (hCPA4) and an inhibiting pro-domain (PD).
This gene is a member of the carboxypeptidase A/B subfamily, and it is located in a cluster with three other family members on chromosome 7. Carboxypeptidases are zinc-containing exopeptidases that catalyze the release of carboxy-terminal amino acids, and are synthesized as zymogens that are activated by proteolytic cleavage. This gene could be involved in the histone hyperacetylation pathway. It is imprinted and may be a strong candidate gene for prostate cancer aggressiveness.
, carboxypeptidase A4-like
, carboxypeptidase A3