cAMP
cAMP, here the cathelicidin antimicrobial peptide encoded by the CAMP gene, is a secreted member of the cathelicidin family with roles in innate immune defence. It is also known as CAP18, FALL39, FALL-39 and LL37. Browse Assay Genie's current range of cAMP research reagents below, or read on for the biology behind the target.
cAMP is an antimicrobial peptide that contributes to innate immune defence. UniProt records that it inhibits the growth of E. coli and B. megaterium and exhibits haemolytic activity against human red blood cells. According to the NCBI Gene summary, the encoded protein has antibacterial, antifungal and antiviral activities, and plays an important role in innate immunity defence against viruses. It also functions in cell chemotaxis, immune mediator induction and the regulation of inflammatory responses, so it links direct antimicrobial action with immune signalling.
The cAMP protein belongs to the cathelicidin family. Family members are characterised by a highly conserved N-terminal signal peptide containing a cathelin domain, together with a structurally variable cationic antimicrobial peptide. The mature antimicrobial peptide is produced by extracellular proteolysis from the C-terminus. UniProt lists the subcellular location as secreted and vesicle, consistent with a peptide that is stored and then released to act outside the cell.
The human CAMP gene is classed by HGNC as a receptor ligand and is named cathelicidin antimicrobial peptide. Historical and alternative names include CAP18, FALL39, FALL-39 and LL37, which may appear in older literature, and the mouse ortholog is Camp. Because the abbreviation cAMP is also widely used for cyclic adenosine monophosphate, researchers should check gene and protein identifiers when searching for this target.
cAMP is an antimicrobial peptide with a recognised role in innate immune defence, including defence against viruses.
As a cathelicidin, cAMP inhibits the growth of bacteria such as E. coli and B. megaterium and has antifungal and antiviral activities.
cAMP functions in cell chemotaxis, immune mediator induction and the regulation of inflammatory responses, making it relevant to immune signalling.
The mature peptide arises by extracellular proteolysis from a cathelin domain-containing precursor, offering a model for studying processing of secreted host-defence peptides.
cAMP is a host-defence peptide. It inhibits the growth of E. coli and B. megaterium, shows haemolytic activity against human red blood cells, and has antibacterial, antifungal and antiviral activities. It also contributes to cell chemotaxis, immune mediator induction and regulation of inflammation.
No. Here cAMP is the cathelicidin antimicrobial peptide encoded by CAMP. Aliases include CAP18, FALL39, FALL-39 and LL37. The abbreviation is shared with cyclic adenosine monophosphate, so use the gene symbol or UniProt accession P49913 to avoid confusion.
Cathelicidins form a family defined by a conserved N-terminal signal peptide with a cathelin domain and a variable cationic antimicrobial region. A mouse ortholog, Camp, is recognised. Check the datasheet of any product for its validated reactivity.
Other antimicrobial peptides, innate immunity effectors and inflammation-associated proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P49913; product specifications from Assay Genie datasheets.